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Biomolecules - 1

INTRODUCTION :
Living matter of cell is called protoplasm.
Protoplasm (Gr. Protos-first+ Plasma-organization) is a living organized substance which is the place
for all physical and chemical transformations, as a characteristics of life.
Protoplasm also includes membranes, cytoplasmic contents and nucleus.
Protoplasm is “physical basis of life”.
Protoplasm is the medium & source of all biological activities.
Protoplasm basically differentiates a nonliving from living.

HISTORY :
Corti (1772) observed protoplasm first time.
Felix Dujardin (1835) studied the jelly-like substance in protozoa and called it sarcode. i.e. flesh of
cell.
J.E. Purkinje (1840) coined the term protoplasm for the living substance.
Hugo von Mohl (1846) applied this name (protoplasm) for the contents of the embryonic cells of the
plants.
Max Schultze (1863) stated that protoplasm is the physical basis of life.
Hanstein (1880) proposed the term protoplast for such organized mass of protoplasm, without cell
wall in plants.
O. Hertwig (1892) propound the protoplasmic theory according to which all living matter, out of which
animals and plants are formed, is protoplasm.
Fisher, Hardy and Wilson (1916) proposed colloidal theory of protoplasm.

PHYSICAL NATURE OF PROTOPLASM


Protoplasm is a greyish, translucent, jelly-like, odourless and viscous substance.
Protoplasm is heavier than water.
Protoplasm behaves as a moderate conductor of electricity.
Size of colloidal particles is 0.001 to 0.1 m.
Mineral ions and smaller inorganic and organic molecules (sugar, salts, simple acids, bases etc.)
occurs as crystalloid solutes in the protoplasm, while larger, organic molecules (proteins, polysac
charides and nucleic acid) occur as colloidal solutes. Thus protoplasm is crystallo-colloidal
mixture.
Scientists call it a “mixture of mixtures”, or “supermixture”.
Protoplasm is a reversible colloidal system i.e. it can change from a thicker, highly viscous “gel”
state to a comparatively more fluid and less viscous “sol” state and vice-versa.
Being a liquid mixture, the protoplasm has a surface tension.
Viscosity = 2 – 20 centipoises.
Refractive index = 1.4

Physical appearance of Protoplasm :


Old theories : Protoplasm appears differently in different
phases.
Alveolar theory-Butschli (1892) : Protoplasm consists
of bubbles or alveoli of a fluid of lesser density
distributed in a fluid of greater density.
Granular theory : Altmann(1893) : The protoplasm
consists of numerous fine granules dispersed
uniformly in homogeneous fluid medium.
Fibriller theory-Fisher (1894) and Flemming (1897)
This theory maintains that protoplasm consists of
numerous minute fibrils or thread-like structures
dispersed in a fluid medium.
NEET_BIOMOLECULES-1 - 1
Reticular theory-Hanstein, Klein and Carnoy : According to this theory protoplasm consists of
numerous minute fibrils which forms a network or reticulum in a fluid medium.

MODERN COLLOIDAL THEORY :


This was first suggested by R.A. Fisher (1894) and latter by Hardy (1899) and Wilson (1916).
It consists of a fluid matrix or ground substance (liquid phase) dispersion phase and dispersed
phase of granules and globules.
The solid and semisolid particles range in diameter from 0.001 to 0.1 (1 or micron = 1/1000 mm.)
The particle are too big to form a suspension and are too small to form a true solution, they thus
remain in the matrix forming a colloidal system.
The liquid phase or dispersion phase of protoplasmic colloids consists mainly of water having dis
solved inorganic ions, salts and small molecules.
The dispersed phase comprises mainly of large molecules of proteins, lipids and carbohydrate.
Phase reversal in protoplasm is due to its colloidal nature. Non living colloid are irreversible in
phase change. (Gel Sol)
Protoplasm shows elasticity.
Elasticity, viscosity, contractility, rigidity are physical properties due to colloidal nature.
Protoplasm shows viscosity.
Colloidal particles show scattering of light, when a beam of light is passed through colloid it be comes
visible. It is called Tyndall effect.
Colloidal particles show zig-zag or irregular movement. The movements are called as Brownian
movement. It occurs during sol state.
Protoplasm responds to the stimulus of chemicals, light and heat or mechanical and thus it shows irrita-
bility.
Protoplasm shows conductivity of impulse produced by stimulus.
All colloidal solution shows ageing. After some time (age) various activities stops.

MOVEMENTS OF PROTOPLASM
It can show following types of movement:
Amoeboid movement :
Naked mass of protoplasm shows creeping movement to form pseudopodia. e.g. Amoeba, Slime
moulds, Neutrophils.
Cyclosis :
Streaming movement of cytoplasm is called cyclosis. It is of two types.
(a) circulation (b) Rotation

CHEMICAL NATURE OF PROTOPLASM


Elements :
About 36 elements are known to occur in protoplasm.
About 13 elements are found in more quantity. These universal elements are C, H, O, N, Cl, Ca, P,
Na, K, S, Mg, I, Fe.
Carbon, hydrogen, nitrogen and oxygen are found greatly in the protoplasm and make up 95% of all living
material. Thus they are called major element.
Remaining 23 elements are called trace element. They are in very small amount (about 0.376%). they are
copper, Cobalt, magnese, zinc, chromium molybdenum, boron, silicon, vanadium, nickle, florine, selenium
etc

Elements % amount A comparison of elements present in non-living and living matter


Oxygen 62 Element % Weight of
Carbon 20
Earth's crust Human body
Hydrogen 10
Nitrogen 3 Hydrogen (H) 0.14 0.5
Calcium 2.5 Carbon (C) 0.03 18.5
Phosphorus 1.14 Oxygen (O) 46.6 65.0
Chlorine 0.16 Nitrogen (N) Very little 3.3
Sulphur 0.14 Sulphur (S) 0.03 0.3
Potassium 0.11
Sodium (Na) 2.8 0.2
Sodium 0.10
Magnesium 0.07 Calcium (Ca) 3.6 1.5
Iron 0.01 Magnesium (Mg) 2.1 0.1
Iodine 0.014 Silicon (Si) 27.7 negligible

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COMPOUNDS OF PROTOPLASM :
Although some elements occur in protoplasm as free ions but mostly they are found in the form of different
kinds of compounds.
Average composition of cells

S.No. [A] Inorganic Compounds


1 Water 70-90%
2 Ions (Salts, acids, bases, gases) 1%
[B] Organic
1 Proteins 10-15%
2 Lipids 2%
3 Carbohydrates 3%
4 Nucleic acids 5-7 %

[A] INORGANIC COMPOUNDS :


1. Water :
Most abundant substance of all living organism.
It forms about 70-90% of the cell.
Water is transparent, colourless and odourless.
It has high surface tension, high specific heat, high heat of vaporization.
pH value of water is 7.
The density of water is maximum at 40C.
It freezes at 00C and boils at 1000C.
The molecule of water is composed of 2 atoms of hydrogen and one atom of oxygen linked by covalent
bonds. Bond angle 1040.
Water exists in two forms-
(i) Free water - about 95%
(ii) Bound water - 5%

FUNCTION OF WATER :
Water is an important structural component.
Water gives an ideal medium for chemical reactions. It is a universal solvent.
A number of waste products are eliminated in solution form mainly as urine with the help of water.
Water keeps the surface of tissues and organs moist.
In living organism, water gives a medium for distribution or transportation of living matter.
Water, works as a dispersion phase in the colloidal system of protoplasm.
Its high specific heat prevents temperature hazards due to sudden change.

Water content in different organism and body parts


1 Body of jelly fish 99%
2 Dormant seed 6%
3 bone cells 25-40%
4 Skeleton muscles 75%
5 Embryo 90-95%
6 Dentine of tooth 10%
7 Enamel of tooth 5%
8 Brain cell 90%
9 Nerve cells 80%
2. Mineral salts :
Salts in protoplasm occur in ionised form
Salt responsible for conducitivity & irritibility
Some important minerals and their functions given in below table

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3. Acids and Bases :
They form buffer system & maintain pH of protoplasm (carbonic acid -bicarbonate buffer)
Phosphoric acid (H3PO4) - found in nucleic acids.
Hydrochloric acid (HCl) - found in gastric juice.
4. Gases :
There are four major gases in protoplasm, which remains dissolved in its free water.
These four gases are CO2 > O2 > N2 > H2 (Solubility order)
CO2 is used in synthesis of urea and dissociation of oxyhaemoglobin.
O2 is used in the oxidation of the substance.
H2 is used for ETS.
According to N CER T Biomolecules
All the c arbon com pounds that we get from living tissues c an be called biom olecules.

Those c ompounds which have molecular weights less than one thous and dalton usually referred as
biomicrom olec ules or simply biomolec ules .
Ac id soluble pool contain those com pounds which have molecular weights ranging from 18 to
around 800 daltons (Da) approx imately .
Those m olecules which are found in the acid insoluble fraction is called mac romolecules or
biomacromolec ules.
The acid insoluble frac tion, has only four types of organic compounds i.e., proteins, nucleic acids,
poly sacc harides and lipids. These classes of compounds with the ex ception of lipids, have
molec ular weights in the range of ten thousand daltons and above
The molec ules in the ins oluble frac tion with the exc eption of lipids are polym eric s ubstanc e but
lipid is not a polym er. Lipids are small molecular weight c ompounds , whos e weight do not exceed
800 Dalton.
Biomolec ules which have molecular weight less than one thous and dalton are called
microbiom olec ule or biomolecule, while thos e which are found in acid insoluble fraction called
macromolecule or m acrobiomolecule.
Lipid which is ins oluble in water. These lipids, bec ause of their as sociation with plas ma
membranes separate in the macromolecular frac tion. Hence, lipids are not stric tly
macromolecules .
The acid soluble pool repres ents roughly the cytoplasmic composition. The mac romolec ules from
cy toplasm and organelles bec ome the ac id insoluble fraction. Together they represent the entire
chemical composition of living tissues or organisms .

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[B] ORGANIC COMPOUND :
Four organic compound are found in acid-insoluble pool protein, nucleic acid, carbohydrate, lipid.
There are three main organic compounds in the protoplasm.
In organic compounds, the main bonds exist between C–C and C–H.
Normally, the organic compounds remain suspended or dissolved in the water of the protoplasm.

TYPES OF ORGANIC COMPOUNDS :


There are following types of organic compounds in protoplasm.
Carbohydrates
Amino acids & Proteins
Lipids
Nucleic acid
Enzyme
Vitamins

CARBOHYDRATE

These compounds are made up of carbon, hydrogen and oxygen. Ratio of H & O is 2 : 1.
Carbohydrate are aldehyde or ketone derivatives of polyhydroxy alcohol.
A carbohydrate may contain aldehyde or ketone group and is called aldose or ketose, respectively.
Certain carbohydrates contain some nitrogen, phosphorous, or sulphur.
Carbohydrate are produced by green plants during photosynthesis. About 80 percent of the dry
weight of the plant is made up of carohydrates.
Carbohydrate are also called saccharides or sugar.
Carbohydrate provides 55-65% of total energy required.
Caloric value - 4.1 Kcal/gm
Storage site - mostly liver and muscles
Daily requirement - 500gm approx.

Types of carbohydrate : Carbohydrates are of three types.


[A] Monosaccharides [B] Oligosaccharides [C] Polysaccharides

(A) Monosaccharides :
These are simple sugars.
Monosaccharides are the simplest and smallest carbohydrates.
These are colourless or white, mostly sweet and crystalline solids which are freely soluble in water.
Monosaccharide molecules have the general formula, C nH2nOn or Cn (H2O)n.
They do not undergo hydrolysis but oxidises to CO2 & H2O.
They contain 3 to 7 carbons.
Suffix - Ose is used in their nomenclature.

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On the basis of nature of functional group they are classified in two groups.
(a) Aldoses : They have aldehyde group (–CHO).
(b) Ketoses : They have ketone group (–C=O).
Classification based on number of Carbon atoms.
(i) Trioses :They have 3 carbon atoms, C3H6O3 e.g., dihydroxyacetone and glyceraldehyde.
(ii) Tetroses : Tetroses contain 4 carbon atoms, C4H8O4 e.g. erythrose, erythrulose.
(iii) Pentoses : They contain 5 Carbon atoms, C5H10O5 e.g. ribose, deoxyribose, xylose, ribulose, arabi-
nose (Gum arabic).

Furanose - Five member ring sugar e.g. Ribose (C5H10O5).

(iv) Hexoses : They have 6 carbon atoms, C6H12O6 e.g. glucose, fructose, galactose and mannose.
In aqueous solutions glucose occur in cyclic structure.

Pyranose - Six member ring sugar e.g. Glucose (C6H12O6).

(v) Heptoses : They have 7 carbon atoms C7H14O7 e.g. sedoheptulose.

Few Important Monosaccharide :


1. Glucose :
Glucose is dextrorotatory so it is called “dextrose”.
Glucose is aldose sugar having –CHO group.
Glucose is found in grapes in abundant quantity so it is also known as “Grape sugar”.
Glucose is the main - respiratory substrate in the body.
Other types of hexose are converted into glucose in liver.
2. Fructose :
Fructose is Levorotatory so it is called “Levulose”.
Fructose is a ketose sugar having C=O group.
Fructose is found in honey (32-40%) and sweet fruits so it is called as “Fruit Sugar”.
Fructose is the sweetest natural sugar.
Fructose is source of energy for sperms and semen.
3. Galactose :
Galactose is not found in free state- In mammalian body galactose is found in milk sugar lactose.
Galactose is also found as a component of galactolipids. i.e. In cerebroside & ganglioside.
4. Mannose :
Mannose is not found in free state.
Mannose occurs in albumin of egg and in wood as component of hemicellulose.
5. Ribose and Deoxyribose :
They are found in nucleic acid, ATP, NAD, NADP, FAD, FMN, Vitamin B 2.

(B) Oligosaccharide :
Oligosaccharides are formed by condensation of 2 to 10 molecules of monosaccharide.
Oligosaccharides on hydrolysis yields 2 to 10 monosaccharide units (monomers).
In oligosaccharides, monosaccharides are linked together by glycosidic bonds.
Aldehyde or ketone group of one monosaccharide reacts with alcoholic group of another monosaccharide
to from glycosidic bond.
One molecule of H2O eliminates during glycosidic bond formation.

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Types of Oligosaccharides :
Disaccharide :
They are formed by condensation of two molecules of monosaccharides e.g. sucrose, maltose, lactose.
Trisaccharides :
They are formed by 3 monosaccharide molecules e.g. raffinose, rhaminose and gentianose.
Tetrasaccharides :
They are formed by condensation of four molecules of monosaccharides e.g., scorodose and stachy-
ose.
Pentasaccharide e.g. verbinose, barbacose (Galactose + Galactose + Glucose + Glucose + Fructose)

Important Disaccharides :
(1) Sucrose (cane sugar) :
Sucrose is obtained from sugar cane and sugar beet, called cane sugar.
Sucrose is a commercial sugar.
It is the storage product of photosynthesis in these plants.
Sucrose is formed by the condensation of
one molecule each of glucose and fructose
with the removal of one molecule of water. ( -
D-Glucose + -D fructose)
1, 2 glycosidic bond is formed between glu-
cose and fructose.
C6H12O6 + C6H12O6 C12H22O11 + H2O
Glucose Fructose Sucrose

(2) Lactose (Milk Sugar) :


Lactose or Milk sugar is found naturally in
mammalian milk.
Lactose is a reducing sugar.

Lactose is formed inside mammary glands by


condensation of one molecules of each of
glucose and galactose ( -D glucose + -D-
galactose)
Lactose have -1- 4 glycosidic linkage
between glucose and galactose.

(3) Maltose (Malt sugar) :


Maltose or malt sugar is found in germinating
starchy seeds.Maltose is formed by
condensation of two molecules of -D glucose
and -D glucose by a 1, 4 glycosidic bond is
formed between two molecules of glucose. It
is reducing sugar.
Functions of Simple Carbohydrate :
Glucose acts as most common respiratory substrate.
Glucose is the blood sugar of many animals.
Mammary glands synthesis lactose of milk from glucose and galactose.
Glucose is utilised in the synthesising fats and amino acids.
Trioses, tetroses, pentoses and heptoses are intermediates in the path way of photosynthesis.

(C) Polysaccharides :
These are complex carbohydrates.
They are formed by polymerisation of 11 to thousands of monosaccharide monomers.
n(C6H12O6) ––– (C6H12O6)n + nH2O
Monosaccharide Polysaccharide
General formula (C6H10O5)n

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They are tasteless and soluble in water.
Suffix-ans is used in nomenclature. Normally they are called as glycans. (Polymers of glucose)
In a polysaccharide chain (like glycogen), the right end is called the reducing end and the left end is
called non-reducing end.
Depending upon the composition, polysaccharides are of two types.
(a) Homopolysaccharides or Homoglycans
Made up of only one type of monosaccharide monomers. For example - starch, cellulose and glycogen,
inulin
(b) Heteropolysaccharides or Heteroglycans
These are formed by condensation of either monosaccharide derivatives or more than one type of
monosacharide monomers. e.g., chitin, agar, hemicellulose, arabagalactans, arabaxylans,
pectin etc.

Based on function, polysaccharide are grouped into three categories: Storage and structural.
(i) Food storage polysaccharides :
They are those polysaccharides, which act as reverve food in the living organisms.
The main storage polysaccharides are starch, glycogen and inulin.

(1) Starch :
Starch is the reserve food in plants.
It is also called amylum.
It is found in abundance in cereal grains (wheat, rice, maize), legumes (pea, gram, beans), potato,
banana etc.
Starch consists of two components: amylose and amylopectin (both glucose polymers).
Amylose is more soluble in water but amylopectin is insoluble.
Amylose have 250-300 glucose units are arranged in an unbranched chain by 1-4 linkage.
Amylopectin is a branched chain molecule. Approximately 30 glucose units are linked in one branchby -
1,4 and -1,6 linkage.
Starch can hold I2 molecules in the helical portion and starch-I2 is blue in colour.
Starch present in potato contains 20% amylose and 80% amylopectin.

(2) Glycogen
It is a main reserve food in animals, bacteria and fungi.
It is also known as animal starch.
Glycogen is stored in muscle cells and liver cells.
Liver of an adult human may store upto 0.91 kg of glycogen.
Glycogen gives red colour with iodine.

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(3) Inulin
Linear polymer of fructose units linked with -1,4 bonds, Inulin is found in roots of Dahalia and
Artichoke.
It is water soluble polysaccharide.
It is not metabolised in human body and filtered through kidney. It is therefore, used in testing of
kidney function, (glomerular filtration).

(ii) Structural polysaccharides :


(1) Cellulose :
It is a homopolysaccharide of -D glucose, having 1, 4 glycosidic bonds. The chains are unbranched.
It is the main structural component of cell wall of plants, some fungi and protists.
Tuncin of tunicate (marine chordate) is related to cellulose (also called as animal cellulose)
Cellulose is the most abundant organic substance of the plants & also on earth.
Cotton fibres have about 90% of cellulose & Wood contain 25-50% of cellulose.
Cellulose is fibrous polysaccharide with a high tensile strength.
A cellulose molecule consists of an unbrached and linear chain of 6000 or more glucose residues with
molecular weight between 0.5 to 2.5 millions.
Cellulose form the bulk of human food and most of the herbivorous.
It can not digested by the human beings, because they lack the enzyme cellulase, required to digest
cellulose.
Cellulose is an important constituent of diet of ruminats such as cows and buffaloes.
Cellulose rich wood is used in production of paper and as fuel.
Cellulose containing fibres of cotton, linen and jute are used for textile and ropes.
Cellulose nitrate is used in propellant explosives.
Cellulose does not contain complex helices and hence cannot hold 2.

(2) Chitin :
Chitin is the second most abundant organic compound in nature.
It is present in the exoskeleton of arthropods and in the cell walls of fungi.
In fungal walls, the chitin is often known as fungus cellulose.
The monomer of chitin is not glucose but nitrogen containing glucose derivative known as N-acetyl
glucosamine.

(3) Pectin :
It is a heteropolysaccharide composed of sugars arabinose and galactose.
Pectin found in cell wall where it binds with cellulose fibrils in bundles.
Salts of pectin i.e. Ca and Mg-pectates form middle lamella in plants.

(4) Hemicellulose :
It is mixture of polysaccharides xylans, galactans, arabagalactans and glucomannans.
It is found in the cell wall. It is hardest known carbohydrate.

(5) Hyaluronic acid (Animal cement) :


It is found in skin, vitreous humour of the eye, the umbilical cord, synovial fluid.
It is a linear polymer of disaccharide repeat units linked with the help of -1,4 glycosidic bonds.
Disaccharides repeat units are D-glucoronic acid and N-acetyl -D- glucosamine.

(6) Chondriotin sulphates :


They are found in cornea, cartilage, tendons, skin, heart, saliva etc.
The repeating unit is a disaccharides consisting of glucoronic acid and sulphate ester of N-acetyl
galactosomines, linked through a -1,3 bond. The disaccharides are linked with each other by -1, 4
bonds.

(7) Heparin :
It is secreted by mast cells in the intestinal mucosa, liver, lung, spleen and kindey.
It is an anticoagulant.

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(8) Agar-Agar :
It is a polysaccharide found in few red algae such as gracillaria, gelidium etc. It is made up of sulfated
galactose. It is important as tissue culture medium.

(9) Tunicin :
It is cellulose like glycan. It costitutes exoskeleton like covering on Urochordata.

(iii) Mucopolysaccharides :
They contain acidic or aminated polysaccharide formed from galactose, mannose, sugar derivatives and
uronic acids.
These are jelly like compounds important in packing and connection.
Mucopolysaccharides are found in the cell walls of bacteria and in the connective tissues of animals
as well as in body fluids.
Hyaluronic acid, chondriotin sulphate and heparin are comon mucopolysaccharides.

Function of Carbohydrate :
They are the primary source of energy.
Normally body obtains 58 to 65% of its required energy from the carbohydrate.
Ribose & Deoxyribose are used in the fromation of RNA, DNA, ATP, NAD, FAD etc.
Starch in plants & glycogen in animals are the stored form of food.
Cellulose is used in the formation of cell wall.
Chitin forms exoskeleton in arthropods and few fungal cell wall.
Heparin (in human blood), Mosquitin & herudin (in herudinaria) act as anti-coagulants.
Chondriotin sulphate is a component of cartilage, tendons & bones, heart valves.

PROTEIN
Protein name is derived from a greek word proteioses which means “holding first place” (Berzelius
and Mulder).
Essential elements in protein are C, H, O, N, (sulphur is also present in less amount)
After water, proteins are most abundant compounds in protoplasm. (10-15%) Amount of proteins is
different in different sources -20% in muscle, 7% in blood plasma, 3.5% in cow milk, 12% in cereal
grain, 20% in nuts and pulses, 11-13% in white part of egg. 15-17 % in yellow part of egg.
Different elements in simple proteins have following proportion-
Carbon- 50-55%, Hydrogen- 7%, Oxygen- 20-24%, Nitrogen-14-18%, Sulphur- 0.3-0.5%.
Caloric value - 5.6 kcal/gm
Daily requirement - 70 - 100gm
Proteins are polymer of amino acid (Fisher and Hofmeister).

Do You Know
1 Protein is a heteropolymer and not a homopolymer.

2 Collagen is the most abundant protein in animal world.


3 Ribulose bisphosphate carboxylase-Oxygenase (RUBISCO) is the most
abundant protein in the whole of the biosphere.

Amino Acid :
Amino acids are organic acids.
All amino acids contain carboxylic acid group and amino acid group, both linked to a single carbon atom
called carbon.

NEET_BIOMOLECULES-1 - 10
Number of known amino acids are more than 100.
Only 20 amino acids are commonly found in proteins of organism. (Magic 20)
These 20 amino acids can be classified into two types.

Semi essential amino acids- Are those amino acids which are synthesized in animal cells but not in
sufficient quantity, thus there presence in food is essential. They are - Arginine and Histidine.
Amino acids are amphoteric compound which exhibits both the acidic (due to –COOH group) and basic
(due to –NH2 group) properties. It is also called as dipolar or zwitter ions.

When R group of such proteinaceous amino acids could be a hydrogen, then amino acid is called
glycine, if methyl group then alanine amino acid and if hydroxy methyl in place of R group then amino
acid is serine and their structures are

Classification of Amino acids :


Amino acids can be classified into three groups depending on their NH2 or –COOH group number.
(1) Neutral
(2) Acidic and
(3) Basic

Neutral amino acids :


This comprises the largest group and can be further subdivided into aliphatic, aromatic, heterocyclic and
sulphur containing amino acids. They have all of them one amino and one carboxylic group, each.

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A. Aliphatic amino acids : H
|
Glycine (Gly) G H – C – COOH
(Aminoacetic acid) |
NH2

Valine (Val) V
( -aminoisovaleric acid)

B. Aromatic Amino acids

Phenylalanine (Phe) F
( -amino, -phenyl propionic acid)

Tyrosine (Tyr) Y
(p-hydroxyphenylalanine)

Tryptophan (Trp) W
( -amino, -indole propionic acid)

C. Heterocyclic amino acid

Cysteine (Cys) C
(a-amino, b-mercapto propionic acid)

II. Acidic amino acids :

Glutamic acid (Glu) E


( -aminoglutaric acid)

III. Basic Amino Acids :

Lysine (Lys) K
( , -diaminocaproic acid)

Structure of proteins :
(1) Primary structure :
A straight chain of amino acids linked by peptide bond form primary structure of proteins.
This structure of proteins is most unstable.
Newly formed proteins on ribosomes have primary structure.

NEET_BIOMOLECULES-1 - 12
(2) Secondary structure :
Protein molecules are spirally coiled.
In addition to peptide bond, amino acid are
linked by hydrogen bond formed between
oxygen of carboxylic group and hydrogen of
amide group. This structure is of two types-

(i) -Helix :
Right handed rotation of spirally coiled chain
with approximately 3½ amino acid in each trun.
This structure have intramolecular hydrogen
bonding i.e. between two amino acid of same
chain e.g. Keratin, Myosin, Tropomyosin

(ii) -Helix or -pleated structure :


Protein molecule have zig-zag structure.
Two or more protein molecules are held together
by intermolecular hydrogen bonding,
e.g. fibroin (silk).

Proteins of secondary structure are insoluble in water and fibrous in appearance. Keratin is a fibrous,
tough resistant to digestion, sclero protein. Hardness of keratin is due to abundance of cystein amino
acid in its structure.

(3) Tertiary structure-


Proteins of tertiary structure are
highly folded to give a globular
appearance. Mostly are water soluble.
This structure of protein have following
bonds-
(i) Peptide bonds
(ii) Hydrogen bonds
(iii) Disulphide bond
(iv) Hydrophobic bond
(v) Ionic bond

NEET_BIOMOLECULES-1 - 13
The tertiary structure of the protein molecules are so arranged as to hide non-polar sides inside and
expose the polar side chains.
Majority of proteins and enzymes in protoplasm exhibit tertiary structure.

(4) Quaternary structure:


Two or more poly peptide chains of tertiary structure
unit by different types of bond to form quaternary struc-
ture of protein.
Different polypeptide chains m ay be similar
(lacticdehydrogenase) and disimilar types (Haemoglo-
bin, insulin).
Quaternary structure is most stable structure of pro-
tein.
Adult human haemoglobin consists of 4 subunits two of
these are identical to each other. Hence, two subunits of
type and two subunits of type.

Properties of proteins :
Proteins are large sized molecules.
Many protein form colloidal solutions.
A protein may bind as well as react with a variety of chemicals.
Proteins can not pass through cell membranes.
The distruption of bond of tertiary proteins structure is called denaturation.
Types of Proteins :
Protein are of three types-
(i) Simple proteins (ii) Conjugated proteins (iii) Derived proteins

(i) Simple Proteins :


They are made up of only amino acids.
They are of two types - Fibrous and globular proteins.
1. Fibrous proteins :
They are thread like structural proteins.
Fibrous protein generally contain secondary structure and are insoluble in water e.g., collagen of
connective tissue, actin and myosin of muscles, keratin of scales, feathers, hairs, claws, nails,
horns and hoofs, silk of spider web.
2. Globular proteins :
They are spherical non-contractile proteins which may be enzymatic or non-enzymatic.
They have tertiary or quaternary structure.
Smaller globular proteins are usually soluble in water and are not coagulated by heat e.g., histones.
Egg albumin, serum globulins and glutelins are examples of large globular proteins, which get coagulated
by heat.
(a) Albumins :
They are water soluble and occur as serum albumin in blood plasma and loctoalbumin in milk.

NEET_BIOMOLECULES-1 - 14
(b) Globulins :
They are soluble in weak acids and alkaline solution but insoluble in water e.g. lactoglobulin in milk.
(c) Histones :
They are water soluble and are rich in lysine and arginine (amino acids) they occur in eukaryotic DNA.
(d) Protamines :
These water soluble arginine rich proteins occur in DNA of spermatozoa of some fishes e.g. salmine in
Salmon.
(e) Gluteins :
They occur only in plants like wheat e.g., glutenin.
(f) Prolamines :
They occur only in plants e.g., zein in corn and gliadin in wheat.
(ii) Conjugated proteins :
These are formed by the binding of a simple protein with a non-protein called the prosthetic group.
These are of following types-
(a) Chromoproteins :
These proteins contain pigment (coloured) as prosthetic group e.g., haemoglobin, haemocyanin, cyto-
chrome, flavoprotien and rhodopsin.
(b) Glycoproteins :
Contain protein + carbohydrate less than 4% eg., plasma glycoprotein secreted from liver and immuno-
globulin produced by lymphocyetes.
(c) Mucoprotein :They have carbohydrate more than 4% e.g., Muerins of bacteria cell wall ossomucoid in
bones, tendenomucoid in tendons, chondromucoid in cartilage. Various mucoproteins are found in
vitrous humor synovial fluid.
(d) Nucleoproteins :
Contain protein + nucleic acid. e.g., histone and non-histone protein join with DNA to make chromo-
somes.
(e) Metalloproteins :
Contain protein + metal ions e.g., Arginase (Mn & Mg), Carbonic anhydrase (Zn), Tyrosinase (Cu),
Xanthine oxidase (Mo) etc.
(f) Phosphoproteins :
Contain protein + phosphate e.g., casein in milk and ovo-vitellin in eggs.
(g) Lipoproteins :
Contain protein + lipids e.g., high density lipoprotein (HDL), low density lipoprotein (LDL) and very low
density lipoprotein (VLDL). Mostly important in membranes.

(iii) Derived proteins : These are denatured or hydrolysed protein.


Primary derived protein : Denatured product e.g. Fibrin, Myosan
Secondary derived protein : Digestion product of proteins eg. Peptones, Proteose di & tripeptide.

Function of proteins :
1. Structural proteins :
Many proteins serve as building material of
cells and tissues.
Some proteins form supporting structures e.g.,
elastin of ligaments, collagen of tendons,
cartilages, cartilage bone and connective
tissue.
2. Protective structure :
Fibrous protein keratin is the major constitu-
ent of external protective structure of animals
like hair, feather, horny layer of skin, nails,
claws, hoofs etc.

NEET_BIOMOLECULES-1 - 15
3. Enzymes :
Many proteins function as enzymes to catalyse biochemical reactions.
4. Carrier proteins :
Some proteins act as carriers which bind and transport specific molecules across a membrane or in a
body fluid.
Haemoglobin transports oxygen in the body.
-globulin of blood carries thyroxine, bilirubin and -globulin transport vitamin A, D and K.
5. Receptor proteins :
A number of proteins present on the external surface of cell membrane act as receptor molecules.
6. Hormones :
Some hormones are proteinaceous e.g., insulin
7. Contractile proteins :
Myosin and actin make the muscle fibres contractile to bring about movements and locomotion.
8. Defence :
Some proteins act as antibodies that participate in the defence mechanism of the body.
9. Storage proteins :
These occur in milk, eggs and seeds to nourish the young ones.
Iron storing protein commonly found in animal tissue is ferritin.
10. Protein Buffers :
Proteins also help in maintaining a balance of acidity and alkalinity by combining with excess acids and
bases.
11. Visual pigments :
Rhodopsin and iodopsin are protein pigments.
12. Toxins :
Many toxins of microbes, plants and animals are proteins.
13. Blood clotting proteins :
The proteins fibrinogen and thrombin help in blood clotting to check bleeding from injuries.
14. Sweetest substance :
Monellin, a protein derived from an African berry in 2000 times sweeter than sucrose.
15. Repressor :
Most of the repressor that regulate gene (operon concept) are protein in nature.

NEET_BIOMOLECULES-1 - 16
LIPIDS

They are made of carbon, hydrogen and oxygen. hydrogen and Oxygen ratio is never same as H 2O.
The number of oxygen atoms in a lipid molecule is always less than number of hydrogen and carbon
atoms.
Sometimes small amount of phosphorus, nitrogen and sulphur are also present.
Lipids are esters of fatty acids and related substances.

They include substance like cooking oil, butter, ghee, natural rubber,
cholesterol etc.
Lipids exhibit a variety of structures but have certain common
characteristics.
Lipids are insoluble in water. But soluble in organic solvents like
chloroform, benzene and acetone.
The basic components of all lipids are fatty acids and many lipids have
both glycerol (tri hydroxy propane) and fatty acids.
Structure of Glycerol

Calorific value - 9 Kcal/gm


Storage site – subcutaneous fat, adipose cells
Daily requirement – 50gm
Lipids in protoplasm are about 2%. These are present as small globules
in protoplasm.
They do not undergo further polymerisation.

NEET_BIOMOLECULES-1 - 17
Fatty acids :
Fatty acids are organic acids with a hydrocarbon chain ending in
carboxylic group (–COOH).
The hydrocarbon chains of fatty acid may possess straight or ring
structure.
Most fatty acids have an even number of carbon atoms between
14 and 22, mostly 16 or 18.
Plants and few animals can synthesis all types of fatty acids.
Some animals including man cannot synthesis few fatty acids eg. linoleic
acid, linolenic acid and arachidonic acids. These fatty acid are called
essential fatty acids (EFA). They obtain these fatty acids through edible
oils eg. sunflower, groundnut cotton seed, coconut oils etc.
Fatty acids are of two types:
(i) Saturated fatty acids
(ii) Unsaturated fatty acids

(i) Saturated Fatty acids :


They do not have double bonds in their carbon chains.
They have higher melting points and are solid at normal temperature.
Saturated fatty acids have general formula CnH2nO2.
The most common fatty acids are e.g., palmitic acid (C16H32O2) or
CH3(CH2)14COOH or C15H31–COOH and stearic acid (C18H36O2) or
CH3(CH2)16COOH or C17H35–COOH
Animals that living in warm climate have large quantity of saturated fatty acids.

(ii) Unsaturated fatty acids :


They have one or more double or triple bonds in their carbon chains.
Most common unsaturated fatty acids are e.g., Oleic acid (C18H34O2),
linoleic acid (C18H32O2) and arachidonic acid (C20H32O2). (most essen-
tial fatty acids)
The unsaturated fatty acids have lower melting points and are liquid at normal temperature.
More unsaturated fatty acids are found in higher plants and in animals that live at low temperature.
In hydrogenation unsaturated fatty acids are changed to saturated and the oil becomes a solid fat.

Do You Know
1
Oils have lower melting (e.g., gingely oil) and hence remain as oil in winters.
2 The fatty acids are found esterified with glycerol. They can be then
monoglycerides, diglycerides and triglycerides.
3 O
CH2–O–C–R 1
R2–C–O–CH O
CH2–O–C–R 3

Structure of Triglyceride
(R1,R2 and R 3 are fatty acids)

Classification of lipids :
Bloor (1943) classified lipids into three types-simple, compound and derived.
(i) Simple lipids :
Simple lipids are formed of fatty acids and trihydric alcohol (glycerol) only.
Simple lipids are of following types-
1. Neutral or true fats- (Glycerides and triglycerides) :
Fats are esters of fatty acid and glycerol.
Each molecule of glycerol can react with three molecules of fatty acids.
Fatty acid (3 molecules) + glycerol (one molecule) Lipid (one molecule) + water (three molecule)
Triglycerides are the most common fats in cells.
Mono-and di-glycerides occur as intermediates in certain biosynthetic reaction.
The three fatty acids are similar only in few fats. They are called pure fats.
Most fats have dissimilar or two of the three fatty acids are similar. They are called mixed fats, (e.g.,
butter)
NEET_BIOMOLECULES-1 - 18
Depending on the physical nature, fats are differentiated into oils and hard fats.
(A) Oils are generally liquid at room temperature.
Oils are rich in unsaturated fatty acids and short chain fatty acids. e.g., groundnut oil, rape seed oil,
mustard oil.
The oils have a tendency to solidify, are called drying oils.
(B) Hard fats are solid at room temperature.
Hard fats contain long chain saturated fatty acids and have high melting point e.g., animal fat.

2. Waxes :
Waxes are highly insoluble esters of long-chain. Monohydroxy alcohol.
Waxes are esters of fatty acids of high molecular weight with alcohol except glycerol.
Waxes have a higher melting point than neutral fats.
Sebaceous glands of mammalian skin secrete waxy sebum which acts as a lubricant to keep the hair and
skin soft.
The sebum secreted by skin glands of wooly mammals is commonly called lanolin or “wool oil”.
Ceruminous and sebaceous glands of the skin that covers the external ear passage in mammals secrete
ear wax.
Spermaceti, a wax found in skull of whale, dolphin.
Honey bees constructed their beehives with bees wax (myricyl palmitate) secreted by their abdominal
glands.
Paraffin wax is obtained from petroleum. Candles are made of paraffin wax and stearic acid.
Carnauba wax (myricyl cerotate) obtained from leaves of carnauba palm.
(ii) Compound lipids :
The compound lipids contain fatty acid, alcohols and other compound as phosphorus, aminonitrogen,
carbohydrates.
Compound lipids are of following types-
1. Phospholipids (Fatty acids + Glycerol + H3PO4 + Other compound) :
These are triglyceride lipids in which one fatty acid is replaced by a phosphate group.
Some phospholipids also have a nitrogenous compound such as choline (in lecithin), ethanolamine (in
cephalin).
Phospholipids are amphipathic carrying both hydrophillic (water attracting) polar and hydropho-
bic (water repellant) non-polar groups because of this property they form bilayers.
In aqueous medium, phospholipid molecules arrange in a double layered membrane or lipid bilayer.
Few examples of phospholipids are-
(a) Lecithin : It is formed by one molecule of glycerol, two molecules of fatty acids and one molecule of
phosphoric acid. Choline is attached with phosphoric acid. Lecithin is found in yolk, brain, soyabean
membrane. It also acts as lipid carrier in blood.

(b) Cephalin : It is like lecithine but choline is replaced by amino ethyl alcohol(Ethanol amine)
Cephalin is found in yolk, blood platelets and Nerve tissues.
(c) Plasmalogens : Occur in vertebrate cardiac muscles, ciliate protists and certain cells of invertebrates.
The plasmalogens is platelet-activating factor (PAF) which is released from basophils (WBC, in Vertebrates)
to stimulate the blood platelets.
(d) Sphingolipid : It is similar to lecithin but have sphingosin in place of glycerol. Sphingomylins are
important as myelin sheath.

2. Glycolipids :
Glycolipids contain fatty acids, and amino alcohol and one or more simple sugars.
The glycolipids are components of cell membranes, myelin sheath of nerve fibres and membrane of
chloroplasts.

NEET_BIOMOLECULES-1 - 19
Animal cells contain cerebrosides and gangliosides.
(a) Cerebrosides : are important lipids of white matter of cells of brain and myelin sheath of the nerve
fibres.
(b) Gangliosides : are found in grey matter of the brain, membraneof RBCs, spleen. They also have
neuraminic acid.
3. Lipoproteins :
Lipoprotein are composed of lipids (mainly phospholipids) and proteins. They are present in the blood,
milk and egg yolk.
4. Cutin and suberin :
Cutin is a complex lipid found in plant cell walls and cuticle. It binds epidermal cells and reduces
transpiration.
Suberin is a mixture of fatty substances. It is present in the wall of cork cells and endodermal cells. It
makes cell wall strong and impermeable to water.
(iii) Derived lipids :
These lipids are obtained by the hydrolysis of simple or compound lipids.
Although these are the products of hydrolysis of lipids, but even then they have some properties of lipids.
Derived lipids are following types.

1. Steroids (sterols) :
Important steroids which have ketone group are called as sterone eg. Testosterone, sterols have – OH
group eg. cholesterol.
Sterols are lipids of high molecular weight e.g., cholesterol, ergosterol, stigmasterol, campesterol etc.
Cholesterol (C27H45OH) is the common sterol found in many animals, human beings and some plants e.g,
Potato.
Cholesterol and its esters are insoluble in water.
Some steroides are hormones like progesterone, estrogen, testosterone and carticosterone.
Cholesterol forms vitamin D on exposure to ultraviolet rays.
Cholesterol in an essential component of animal cell membrane and the cell membrane of mycoplasmas.
Ergosterol and stigmasterol are found in plants, fungi.

3. Terpenes :
Terpenes are lipid like hydrocarbons formed of isoprene (C5H8) units.
They are major components of ‘essential oils’ produced by certain plants.
The terpenes include certain fat soluble vitamins like A, E, K, carotenoids and certain coenzymes like
coenzyme Q.

4. Prostaglandins :
Prostaglandins are hormone like compound derived from 20 carbon polysaturated fatty acids such as
arachidonic acid.
They are present in human seminal fluid, testis, kidney, placenta, uterus, stomach, lung, brain and heart.
The main function of prostaglandins is binding of hormones to membranes of target cells. Regulation of
B.P. gonadial peristalsis and osmoregulation.

NEET_BIOMOLECULES-1 - 20
Function of lipids :
1. Food material :
Lipids provide food, highly rich in calorific value. One gram lipid produces 9 kilocalories of heat.

2. Food reserve :
Lipids are insoluble in aqueous solutions, and therefore can be stored readily in the body as a food
reserve.

3. Structural components :
They make an impotant constituent of the cell membrane.

4. Heat insulation :
The fats are characterised for their high insulating capacity. Great quantities of fat are deposited in the
sub-cutaneous layers in aquatic mammals such as whale and in animals living in cold climates.

5. Fatty acid absorption :


Phospholipids play important role in the absorption and transportation of fatty acids & fat soluble vitamins.

6. Hormone synthesis :
The sex hormones, adrenocorticoids, cholic acids and also vitamin D are all synthesised from choles-
terol, a steroidal lipid.

7. Vitamin carriers :
Lipids act as carriers of natural fat-soluble vitamin such as vitamin A, D and E.

NEET_BIOMOLECULES-1 - 21
Type (I) : Very Short Answer Type Questions : [01 Mark Each]
1. Write the names of microbiomolecule.
2. Write the name of storage food in plant & animal body.
3. Write the name of macromolecule found in acid insoluble fraction.
4. Write the name of various polysaccharides

5.

Write the name of (B) in above structure.

Type (II) : Short Answer Type Questions : [02 Marks Each]


6. Write the name of smallest component of inulin, protein & lipid.
7. Write the definition of biomolecule.
8. Write the name of primary and secondary metabolites.

Type (III) : Long Answer Type Questions: [03 Mark Each]


9. Classify carbohydrates, explain with examples.
10. Write the function of protein.
11. What is Amino acid ? Give the examples of essential & non-essential amino acids

Type (IV) : Very Long Answer Type Questions: [05 Mark Each]
12. What is meant by tertiary structure of proteins ?
13. What are lipids? Described about their types.
14. Draw the structure of any amino acid. Describe with examples neutral, acidic & basic amino acid.
15. Describe the importance of carbohydrate.

OBJECTIVE QUESTIONS
oLrqfu"B iz'u ¼OBJECTIVEQUESTIONS½
PHYSICAL PROPERTIES
1. The dispersed phase of protoplasm, according to colloidal hypothesis, is constituted by-
(1) Inorganic minerals (2) Organic compounds
(3) Organelles (4) All

NEET_BIOMOLECULES-1 - 22
2. The homogenous ground substance of the cell was termed by Altmann as-
(1) Protoplasm (2) Cytoplasm (3) Hyaloplasm (4) None of these
3. Protoplasm is-
(1) True solution (2) Emulsion (3) Suspension (4) Colloidal solution
4. Protoplasm is-
(1) Transparent colloidal and viscous solution (2) Translucent, jelly like and suspended solution
(3) Translucent, jelly like colloidal solution (4) Transparent, jelly like colloidal solution
5. The electrolytes of protoplasm help the cell to maintain its-
(1) Viscosity (2) Phase reversal property
(3) Osmotic pressure & phase reversal (4) Osmotic pressure & pH regulation
6. The response to changes in internal and external environment by protoplasm is called-
(1) Conductivity (2) Irritability
(3) Adaptability (4) All of these
7. The normal concentration of cholestrol in plasma is-
(1) 100·mg to 150 mg /100 ml (2) 150 mg to 250 mg /100 ml
(3) 250 mg to 500 mg /100 ml (4) 300 mg to 500 mg /100 ml
8. Presence of large amount of water in protoplasm-
(1) Helps in shape maintenance (2) Helps in elimination of metabolic wastes
(3) Keeps temperature of cell relatively constant (4) All of the above
9. Brownian movement is due to-
(1) Collision and reversal of electrically charged molecules
(2) Simple movement of molecules themself
(3) Force existing between molecules
(4) Attraction between molecules
10. Protoplasm is made up of-
(1) Cytoplasm & nucleus (2) Cytoplasm & nucleolus
(3) E.R. and Golgi body (4) Mitochondria & plastids
11. In animal a continuous living mass without cell boundaries having many nuclei in it is called-
(1) Syncytium (2) Coenocyte (3) Syngnathus (4) None of these
12. Protoplasm without nucleus is known as -
(1) Cytoplasmic matrix (2) Trophoplasm (3) Cell inclusion (4) Cytoplasm
13. Which of the following is the physical property of protoplasm-
(1) Tyndall's effect (2) Adsorption (3) Phase reversal (4) All of these
14. The growth of an active protoplasm occurs by
(1) Reproduction (2) Cell division (3) Assimilation (4) All
15. A colloidal solution is regularly heated then what will happen to brownian movement:
(1) regularly increase (2) regularly decrease
(3) first increase then decrease (4) first decrease then increase
16. Inter Change of plasmasol and plasmagel is a-
(1) Bio-chemical phenomenon (2) Physiobio-chemical phenomenon
(3) Chemical phenomenon (4) Physical phenomenon
17. Who proposed the name 'sarcode' for protoplasm-
(1) Van mohl (2) Corti (3) Dujardin (4) Schultz

NEET_BIOMOLECULES-1 - 23
18. Which theory is most acceptable for physical structure of protoplasm-
(1) Granular theory (2) Reticular theory (3) Alveolar theory (4) Collodial theory
CARBOHYDRATE
19. Callose is polymer of-
(1) Fructose (2) Sucrose (3) Glucose (4) Xylans
20. Where is glycogen stored-
(1) Liver and muscles (2) Liver only (3) Muscles only (4) Pancreas
21. Which is a disaccharide -
(1) Galactose (2) Fructose (3) Maltose (4) Dextrin
22. Which substance is not carbohydrate -
(1) Starch (2) Glycogen (3) Wax (4) Glucose
23. To get quick energy one should use -
(1) Carbohydrate (2) Fats (3) Vitamins (4) Proteins
24. External coat composed of cellulose like material occurs in - .
(1) Hemichordata (2) Urochordata (3) Cephalochordata (4) Cyclostomata
25. Monosaccharides is -
(1) Pentose Sugar (2) Hexose Sugar (3) Glucose (4) All the above
26. Sugar which is found in haemolymph of insects is called-
(1) Maltose (2) Lactose (3) Trehalose (4) Galactose
27. Starving person will first use from the following-
(1) Fats (2) Glycogen (3) Blood protein (4) Muscle protein
28. Which of the following sugar is found in ATP -
(1) Deoxyribose (2) Ribose (3) Trehalose (4) Glucose
29. Lactose is composed of -
(1) Glucose + galactose (2) Glucose + Fructose
(3) Glucose + Glucose (4) Glucose + mannose
30. True statements for cellulose molecule -
(1) -1-4Iinkage, unbranched (2) -1-4Iinkage, branched
(3) -1-4 linkage, branched. (4) -1-6Iinkage,unbranched
31. Sweetest sugar among the naturally occuring sugar-
(1) Glucose (2) Fructose (3) Sucrose (4) Saccharine
32. Which sugar occur only in mammals -
(1) Trehalose (2) Galactose (3) Lactose (4) Mannose
33. Amylose and Amylopectin occur in -
(1) Glycogen (2) Starch (3) Cellulose (4) Chitin
34. The blood group proteins of man are composed of-
(1) Glycoproteins (2) Mucoproteins (3) Lipoproteins (4) Phosphoproteins
35. Animal starch (glycogen) differs from plant starch in-
(1) Having short chain branched structure (2) Being reserve food of animals mostly
(3) Give no blue colour with iodine (4) All of the above
36. The basic unit of chitin is-
(1) N-acetyl glucosamine (2) Glucose
(3) Galactose (4) Fructose

NEET_BIOMOLECULES-1 - 24
37. The formation of glucose from non-carbohydrate materials is called-
(1) Glycogenesis (2) Glycogenolysis (3) Gluconeogenesis (4) Glycolysis
38. Glucose, galactose and fructose all have the same molecular size and composition and their absorption
through the mucosal cells takes place-
(1) At the same rate (2) Glucose is absorbed most rapidly
(3) Fructose is absorbed most rapidly (4) Galactose is absorbed most rapidly
39. Honey contains the hydrolytic product of-
(1) Lactose (2) Maltose (3) Insulin (4) Starch
40. In human being, galactose is most easily available-
(1) By the conversion of glucose (2) By the conversion of fructose
(3) By the hydrolysis of maltose (4) By the hydrolysis of milk
41. Which of the following is not a mucopolysaccharide-
(1) Heparin (2) Chondroitin sulphate
(3) Hyaluronic acid (4) Inulin
42. The normal blood glucose level of an adult in the post absorptive state is-
(1) 40-60 mg/100 ml (2) 80-100 mg/100 ml
(3) 120-130 mg/100 ml (4) 160-180 mg/100 ml
43. Carbohydrate metabolism is controlled by-
(1) Paratharmone (2) Insulin
(3) Glucose (4) Vitamin B12
PROTEIN AND AMINO ACID
44. Which group is correct:
(1) Glycoprotein - Mucin (2) Salmin - Phosphoprotein
(3) Lipoprotein - Lecithin (4) Cytochrome - Mucoprotein
45. In infants of under 6 months of age, deficiency of protein may cause -
(1) Marasmus (2) Kwashiorkar (3) Rickets (4) Galactosemia
46. Which element is normally absent in proteins-
(1) C (2) N (3) S (4) P
47. Protein most abudant in human body are -
(1) Collagen (2) Myosin (3) Actin (4) Albumin
48. Proteins which are present in protoplasm are very important because -
(1) They provide rigidity to cell (2) They function as biocatalyst
(3) They yield energy (4) They are stored food
49. Products of proteins catabolism -
(1) NH3, CO2 and Urea (2) Urea, CO2 and NH
(3) Urea, NH3 and uric acid (4) Urea, NH3, alanine and creatine
50. Unit of proteins which unite in long chains to form proteins are called -
(1) Sugar (2) Purines (3) Pyrimidines (4) Amino acids
51. Milk protein is -
(1) Lactogen (2) Myosin (3) Casein (4) Pepsin
52. The simplest amino acid is-
(1) Tyrosine (2) Lysine (3) Glycine (4) Aspartic acid

NEET_BIOMOLECULES-1 - 25
53. The amino acids which are not synthesized in the body are called -
(1) Non-essential (2) Essential (3) Deaminated (4) All of them
54. Which of the following will be different in different animals -
(1) Fats (2) Carbohydrates (3) Proteins (4) Vitamins
55. In India the best source for proteins in herbivorous persons is-
(1) Pulses (2) Potato (3) Egg (4) Meat
56. Proteins are transported in the body of herbivorous persons as -
(1) Amino acids (2) Natural proteins (3) Enzymes (4) Nucleic acid
57. The formation of protein can be considered as-
(1) Dehydration synthesis (2) Dehydration analysis
(3) Hydration synthesis (4) Hydration analysis
58. In most of the Amino acid Metabolism the first step is :
(1) Transamination (2) Decarboxylation
(3) Transamidation (4) Deamination.
59. Genetic code determines -
(1) Structural pattern of an organism (2) Sequence of amino acid in a protein chain
(3) Variation in offsprings (4) Constancy of morphological trait.
60. Which of the following amino acid is essential-
(1) Alanine (2) Glycine (3) Tryptophan (4) Tyrosine
61. Which is most important structural part of the body-
(1) Protein (2) Carbohydrates (3) Lipid (4) Nucleic acid
62. Which protein is oxidised by light producing animals:
(1) Gramicidin (2) Leuciferin (3) Flavin (4) Leumin
63. Contractile protein is -
(1) Actin (2) Myosin (3) Troponin (4) Tropomyosin
64. Variations in proteins are due to -
(1) Sequence of amino acids (2) Number of amino acids
(3) R-group (4) None
65. Histone is a basic protein due to -
(1) Alanine & Glycine (2) Methionine & serine
(3) Tryptophan & tyrosine (4) Lysine & Arginine
66. Which amino acid is an important constituent of vitamin folic acid:
(1) Glycine (2) Glutamic acid (3) Argenine (4) Lysine
67. Example of phosphoprotein is-
(1) Mucin (2) Fibrinogen (3) Casein (4) Myosin
68. The essential amino acids-
(1) Must be supplied in the diet because the organism has lost the capacity to aminate the corresponding
keto acid
(2) Must be supplied in diet because the human has an impaired ability to synthesize the carbon chain of
corresponding keto acids
(3) Are indentical in all species
(4) Are defined as those amino acids which cannot be synthesized by the organism at a rate adequate to
meet metabolic requirements

NEET_BIOMOLECULES-1 - 26
69. Which of the following is sulphur containing amino acid-
(1) Alanine (2) Lysine (3) Methionine (4) Argenine
70. Following are Aromatic amino acid
(1) Glycine, Valine, Alanine (2) Phenylalanine, Tyrosine, Tryoptophan
(3) Cysten, Methionine, Glutamic acid (4) Threonine, Leucine, Argenine
71. Which one is not a protein:
(1) Cytochrome (2) Myoglobin (3) Fibrinogen (4) urea
72. Histones are-
(1) Nucleic acids (2) Nitrogen bases of DNA
(3) Proteins of eukaryotes (4) Proteins of prokaryotes
73. Growth repair and protection against diseases in our body is carried by-
(1) Vitamins (2) Hormones (3) Proteins (4) Lipids
74. The process of protein synthesis is also called-
(1) Translation (2) Tranduction
(3) Translation & tranduction (4) Transcription - Translation
75. Amino acids have net charge zero at-
(1) Every pH (2) No pH
(3) A specific pH (4) None of these
76. In many proteins, the hydrogen bonding produces a regular coiled arrangment called-
(1) -helix (2) -helix (3) both (4) None
77. The unwanted amino acid abstracted from the tissues are either used up by the tissue or in the liver
converted into-
(1) Ammonia (2) Urea (3) Ammonium salts (4) Uric acid

LIPIDS
78. Cholesterol is synthesized in -
(1) Pancreas (2) Brunners gland (3) Spleen (4) Liver
79. Long chain molecules of fatty acids are formed by-
(1) Polymerisation of 2 carbon compounds (2) Decomposition of fats
(3) Polymerisation of glycogen (4) Conversion of glycogen
80. Fats in the body are formed when -
(1) Glycogen is formed from glucose
(2) Sugar level becomes stable in blood
(3) Extra glycogen storage in liver and muscles is stopped
(4) All of them
81. Gaucher's disease is concerned with which of the following -
(1) Abnormal fat metabolism (2) Abnormal protein metabolism
(3) Abnormal carbohydrate metabolism (4) None of them
82. Lipid derivative which occur in faecal material -
(1) Cholesterol (2) Ergesterol (3) Lanoline (4) coprosterol
83. Cerebrosides & Gangliosides are -
(1) Phospholipids (2) Chromolipids (3) Glycolipids (4) Sulpholipids

NEET_BIOMOLECULES-1 - 27
84. Lecithin is chemically:
(1) Phosphatidyl choline (2) Phosphatidyl ethanolamine
(3) Phosphatidyl serine (4) Phosphatidyl sphingosin
85. Cholesterol is an important compound in the body, because it-
(1) Regulates blood pressure
(2) Gives rise to steroid hormone
(3) Regulates filtration pressure in kidneys
(4) Is involved in Ca++ absorption from gut
86. Which of the following lipids is most abundant in cell membrane-
(1) Steroid (2) Cholesterol (3) Phospholipid (4) Cutin
87. The “free fatty acid" (FFA) of plasma are-
(1) Metabolically inert (2) Mainly bound to beta lipoproteins
(3) Stored in fat (4) Mainly bound to serum albumin
88. Esters of long chain fatty acid with long-chain monohydric alcohols are called-
(1) Fats (2) Waxes (3) Both of the above (4) None of the above
89. The density of lipoproteins increases as the protein content-
(1) Decreases (2) Increases
(3) Not related with the protein content (4) None of these
90. The majority of the absorbed fat appears in the form of-
(1) HDL (2) LDL (3) VLDL (4) Chylomicrons
91. Human system lacks the enzymes capable of synthesizing-
(1) Oleic acid (2) Archidonic acid
(3) Linolenic acid (4) Linoleic and linolenic acid
92. Which of the following bond formed by dehydration:-
(1) Peptide bond & hydrogen bond (2) Peptide bond & glyco sidic bond
(3) Glycosidic bond (4) All of the above
93. Which of the following is wrong about protein:-
(1) Protein is a polymer of amino acids, which are joined by peptide bond.
(2) A protein is imagined as a liene, the left end respresented by the first amino acid and right end
represented by last amino acid
(3) The first amino acid is called as N-terminal amino acid while last amino acid is called as C-terminal
amino acid
(4) Protein is a homopolymer.
94. Which of the following statement is correct about amino acid:-
(1) These are substituted methanes.
(2) In these amino (–NH2) and carboxyl (–COOH) group are of ionizable nature.
(3) Based on the nature of R-group there are many amino acids
(4) All of the above correct

NEET_BIOMOLECULES-1 - 28
95. Which of the following group contain acid solusble compound?
(1) Polysaccharide, glucose (2) Glucose protein
(3) Sulphate (4) All of the above
96. In amino acid, the name of groups present on all four valancy of -carbon are :-
(1)Hydrogen, Carboxyl, amino and R-group (2) Hydrogen, alcoholic, amino and R-group
(3) Hydrogen, alcoholic, carboxyl and R-group (4) None of the above
97. Decreasing order of amount of organic compound in animal body
(1) Carbohydrate, protein, fat and nucleic acid
(2) Protein, fat, nucleic acid and carbohydrate
(3) Protein fat, carbohydrate and nucleic acid
(4) Carbohydrate, fat, protein and nucleic acid
98. Which of the following compound is most alundant by found in a cell :-
(1) Protein (2) Lipid (3) Carbohydrate (4) Water
99. Which is odd, among the following
(1) Chitin-Carbohydrate (2) Pectin-protein
(3) Steroid-lipid (4) Wax-lipid

OBJECTIVE QUESTIONS
oLrqfu"B iz'u ¼OBJECTIVEQUESTIONS½
1. The statement "All biological catalysts are proteins" is no more valid because of the discovery of :
(FIBNO)
(1) ribonuclease (2) ribozymes (3) lysozymes (4) enzymes
2. Any lens cleaning fluid essentially contains: (FIBNO)
(1) lipase (2) protease (3) cellulose (4) mild detergent
3. Cholesterol: (4th ABO)
(1) plays an important role in controlling the fluidity of cell membranes
(2) holds membrane bound proteins within the lipid bilayer
(3) often has a role as a hormone receptor on the surface of membranes
(4) is a water soluble molecule found in both prokaryotes and eukaryotes
4. A cell membrane contains 60% protein (density 1.33) and 40% phospholipid (density 0.93). When the
membrane is centrifuged in NaCl solution of density 1.03 gm/cm 3, it will: (1st NSEB)
(1) float (2) sediment
(3) layer in the centre of the NaCl Column (4) fragments in the NaCl columns
5. A unit of composed of sugar and nitrogen base linked by glycosidic bond is : (2nd NSO II L)
(1) purine (2) glycoside (3) nucleoside (4) nucleotide
6. Molecules resulting from the hydrolysis of a dipeptide are: (8th CBO)
(1) two sugars (2) an amino acid and an alcohol
(3) an acid and an amine (4) two amino acids

NEET_BIOMOLECULES-1 - 29
7. Which statement about proteins is correct? (4th CBO)
(1) Protein quaternary structure is determined slowly by the primary amino acid sequence
(2) Protein sequences that span a lipid bilayer membrane usually contain a number of charged amino
acids
(3) Examples of protein secondary structure include an helix or a pleated sheet
(4) Protein tertiary structure is the result of the interaction of two or more independent polypeptide chains
8. Water is the most abundant substance in all organisms. Next to water, the major components of living cell
are: (9th CBO)
9. The bonding of two amino acid molecules to form a larger molecule requires: (5th CBO)
(1) the release of a water molecule (2) the release of a carbon dioxide molecule
(3) the addition of a water molecule (4) an increase in activation energy
10. Three properties (i, ii, iii) of an amino acid are given. Study the structure and mark one amino acid which
has all the three properties: (FINBO)
1. Contain an imino group.
2. With ninhydrine formed a yellow derivative.
3. Is a non essential amino acid.

(1) (2)

(3) (4)

11. Fats provide more energy than carbohydrates because - [KVPY_2007_SB]


(1) Fats contain higher percentage of C and H and lower percentage of O than carbohydrates
(2) Fats gets readily oxidized than carbohydrates
(3) Fats contain higher percentage of O than C
(4) Fats can be absorbed readily by our bodies than carbohydrates
12. The effect of consumption of excess protein by normal individuals would result in : [KVPY_2009_SB]
(1) excretion of excess protein in urine
(2) increase in the amount of adipose tissue
(3) increase in the synthesis of muscle protein
(4) increase in the circulatory plasma proteins

NEET_BIOMOLECULES-1 - 30
AIIMS CORNER
1. Cellulose, the most important constituent of plant cell wall is made of [AIIMS-2007]
(1) Unbranched chain of glucose molecules linked by 1, 4 glycosidic bond
(2) Branched chain of glucose molecules linked by 1, 4 glycosidic bond in straight chain and 1, 6
glycosidic bond at the site of branching
(3) Unbranched chain of glucose molecules linked by 1, 4 glycosidic bond
(4) Branched chain of glucose molecules linked by 1, 6 glycosidic bond at the site of branching
2. Jute fibres deteriorate quickly because (AIIMS 2009)
(1) cellulose content is high (2) lignin content is high
(3) cellulose content is low (4) lignin content is low
3. Which of the following sugars is not found in plants? (AIIMS 2009)
(1) sucrose (2) glucose (3) lactose (4) fructose
4. Cotton fibres mainly contains (AIIMS 2009)
(1) cellulose (2) glycogen (3) protein (4) lipid
In each of the following questions a statement of Assertion (A) is given followed by a corresponding
staterment of Reason (R) just below it. Of the statements, mark the correct answer as
(1) If both assertion and resaon are true and reason is the correct explanation of assertion
(2) If both assertion and reason are true but reason is not the correct explanation of assertion
(3) If assertion is true but reason is false
(4) If both assertion and reason are false
5. Assertion (A) : Simple carbohydrates having free aldose or ketose group are called reducing sugars.
Reason (R) : They can reduce cupric ion to cuprus state.
(1) (2) (3) (4)
6. Assertion (A) : Protein amino acids possess an amino group attached to a corbon ( amino acid).
Reason (R) : Proline and hydrolyproline have NH (imino group) so they are imino acids.
(1) (2) (3) (4)
7. Assertion (A) : Linolenic acid is precursor of arachidonic acid.
Reason (R) : Ascorbic acid is sugar acid having NH2 group.
(1) (2) (3) (4)
8. Assertion (A) : In intracellular pool K is most abundant followed by PO4, Mg, CO3, Na, CI and Ca
Reason (R) : Water is most abundant component of protoplasm.
(1) (2) (3) (4)
9. Assertion (A) : Cellulose can be digested by only a few microbes present in the gut of reminants and white
ants.
Reason (R) : Cellulose is the most abundant organic molecule.
(1) (2) (3) (4)
10. Assertion (A) : Total number of amino acids involved in protein synthesis in plants is 20.
Reason (R) : Only 20 amino acids have been discovered so far.
(1) (2) (3) (4)

NEET_BIOMOLECULES-1 - 31
11. dFku (A) : In human body collagen is the most abundent protein.
dkj.k (R) : Scleroproteins occur in hard parts of animal body for providing support and protection.
(1) (2) (3) (4)

PART- 1

1. In which one of the following groups, all the three are examples of polysaccharides [AIPMT 1996]
(1) Starch, glycogen, cellulose (2) Sucrose, maltose, glucose
(3) Glucose, fructose, lactose (4) Galactose, starch, sucrose
2. Conjugated proteins containing carbohydrates as prosthetic group are known as [AIPMT 2000]
(1) Chromoproteins (2) Glycoproteins (3) Lipoproteins (4) Nucleoproteins
3. Which is an essential amino acid [AIPMT 2000]
(1) Serine (2) Aspartic acid (3) Glycine (4) Phenylalanine
4. Most abundant organic compound on earth is [AIPMT 2001, 2004]
(1) Protein (2) Cellulose (3) Lipids (4) Steroids
5. Spoilage of oil can be detected by which fatty acid [AIPMT 2001]
(1) Oleic acid (2) Linolenic acid (3) Linoleic acid (4) Erucic acid
6. Cytochrome is [AIPMT 2001]
(1) Metallo flavoprotein (2) Fe containing porphyrin pigment
(3) Glycoprotein (4) Lipid
7. Element necessary for the middle lamella [AIPMT 2001]
(1) Ca (2) Zn (3) K (4) Cu
8. In plants, inulin and pectin are [AIPMT 2001]
(1) Reserve materials (2) wastes
(3) Excretory material (4) Insect-attracting material
9. Cellulose, the most important constituent of plant cell wall is made of [AIPMT, AIIMS 2000, 2007]
(1) Unbranched chain of glucose molecules linked by 1, 4 glycosidic bond
(2) Branched chain of glucose molecules linked by 1, 4 glycosidic bond in straight chain and 1, 6
glycosidic bond at the site of branching
(3) Unbranched chain of glucose molecules linked by 1, 4 glycosidic bond
(4) Branched chain of glucose molecules linked by 1, 6 glycosidic bond at the site of branching
10. Collagen is [AIPMT 2002]
(1) Fibrous protein (2) Globular protein (3) Lipid (4) Carbohydrate
11. Lipids are insoluble in water because lipid molecules are [AIPMT 2002]
(1) Hydrophilic (2) Hydrophobic (3) Neutral (4) Zwitter ions
12. Which of the following is a reducing sugar [AIPMT 2002]
(1) Galactose (2) Gluconic acid (3) -methyl galactoside (4) Sucrose

NEET_BIOMOLECULES-1 - 32
13. Which steroid is used for transformation [AIPMT 2002]
(1) Cortisol (2) Cholesterol (3) Testosterone (4) Progesterone
14. The major portion of the dry weight of plants comprises of [AIPMT 2003]
(1) Carbon, nitrogen and hydrogen (2) Carbon, hydrogen and oxygen
(3) Nitrogen, phosphorus and potassium (4) Calcium, magnesium and sulphur
15. During anaerobic digestion of organic waste, such as in producing biogas, which one of the following is
left undergraded [AIPMT 2004]
(1) Hemicellulose (2) Lipids (3) Cellulose (4) Lignin
16. Which of the following is the simplest amino acid [AIPMT 2005]
(1) Alanine (2) Asparagine (3) Glycine (4) Tyrosine
17. Antibodies in our body are complex [AIPMT 2006]
(1) Steroids (2) prostaglandins (3) Glycoproteins (4) Lipoproteins
18. Which one of the following is not a constituent of cell membrane [AIPMT 2007]
(1) Cholesterol (2) Glycolipids (3) Proline (4) Phospholipids
19. About 98 percent of the mass of every living organism is composed of just six elements including carbon,
hydrogen, nitrogen, oxygen and. [AIPMT 2007]
(1) Phosphorus and sulphur (2) Sulphur and magnesium
(3) Magnesium and sodium (4) Calcium and phosphorus
20. Which one of the following structural formulae of two organic compounds is correctly identified along with
its related function ? [AIPMT Pre. 2011]

(1) B : Adenine - a nucleotide that makes up nucleic acids


(2) A : Triglyceride - major source of energy
(3) B : Uracil - a component of DNA
(4) A : Lecithin - a component of cell membrane

NEET_BIOMOLECULES-1 - 33
21. Which one out of A -D given below correctly respresents the structural formula of the basic amino acid
[AIPMT Pre. 2012]

Options
(1) C (2) D (3) A (4) B

22. Cellulose form a major portion of food grazing cattle, it is - [AMU 1987]
(1) Digested by bacteria of alimentary canal
(2) Digested by animal itself
(3) Digested partly by the animal and partly by bacteria
(4) Passed out undigested
23. Glycoprotein are known to play important role in cell recognition, the specificity of this recognition is
provided largely by - [CBSE 1990]
(1) Protein portion of the glycoproteins
(2) Carbohydrate portion of the glycoproteins
(3) Both carbohydrate and protein portion of glycoproteins
(4) Lipid portion of glycoprotein
24. The first amino acids taking part in protein synthesis- [CBSE 1992]
(1) Met (2) Val (3)Arg (4) Tryp.
25. Dipeptide is- [RPMT 1993]
(1) Structure of two peptide bonds
(2) Two amino acids linked by one peptide bond
(3) Bond between one amino acid and one peptide
(4) None
26. Decreasing order of amount of organic compound in animal body- [RPMT 1994]
(1) Carbohydrate, Protein, Fat and Nucleic acid
(2) Protein, Fats, Nucleic acid and Carbohydrate and nucleic acid
(3) Protein, Fats, Carbohydrate and Nucleic acid
(4) Carbohydrate, Fats, Proteins and Nucleic acid

NEET_BIOMOLECULES-1 - 34
27. Characteristic feature of haemoglobin- [RPMT 1994]
(1) Reversible union with oxygen (2) Red colour
(3) Presence of Cu (4) Presence of globulin protein
28. Correct about glycogen is that it is- [CBSE 1995]
(1) A disaccharide stored in liver and can react with NH3 to form proteins
(2) Synthesized in liver and takes part in formation of bile and lipase besides being a source of energy
(3) A polysaccharide synthesized and stored in liver cells
(4) Synthesized in blood and stored in liver and muscles to provide glucose in times to need
29. Cotton fibres are made of- [CPMT 1996]
(1) Protiens (2) Starch (3) Lignin (4) Cellulose
30. Most diverse macromolecules found in cells, both physically and chemically are- [CBSE 1996]
(1) Lipids (2) Carbohydrates (3) Proteins (4) Nucleic acid
31. Cellulose is made up of- [CBSE 1998]
(1) Unbranched chain of glucose molecules linked by 1-4 glycosidic bonds
(2) Branched chains of glucose molecules lined by 1-6glycosidic bond in straight chains and 1-6
glycosidic bonds at branch points
(3) Unbranched chains of glucose molecules lined by 1-6 glycosidic bonds
(4) Branched chains of glucose molecules linked by 1-6 glycosidic bonds at branch points
32. Lactose is composed of- [CBSE 1998]
(1) Glucose + galactose (2) Glucose + glucose
(3) Glucose + fructose (4) Fructose + fructose
33. Enormous diversity of protein molecules is mainly due to diversity of- [CBSE 1998]
(1) Peptide bonds (2) Amino groups of amino acids
(3) R groups of amino acids (4) Amino acid sequences within the protien molecules
34. The antibodies are- [MP PMT 1998]
(1) (Gamma) - globulins (2) Albumines
(3) Vitamins (4) Sugar
35. Which is not an essential macro-element for growth of plants- [CPMT 1999]
(1) Na (2) Ca (3) Zn (4) K
36. Most abundant molecule of Nature is- [CPMT 1999]
(1) Glucose (2) Cellulose (3) Starch (4) Ribose
37. Identify the protein which does not contain any metal- [CPMT 1999]
(1) Phytochrome (2) Cytochrome (3) Glycoprotein (4) Ferritin
38. Which one is storage protein- [CPMT 1999]
(1) Ferroprotein (2) Chromoprotein (3) Mucoprotein (4) Glutelin
39. Which protein found in maximum amount- [CBSE PMT 1999]
(1) Catalase (2) Zinc carbonic anhydrase
(3) Transferase (4) RUBISCO
40. Living substance of cells was called "sarcode" by- [CPMT 2000]
(1) Robert Brown (2) Dujardin
(3) Robert Hooke (4) Purkinje

NEET_BIOMOLECULES-1 - 35
41. Saline solution is given to patients of cholera because- [MPPMT 2000]
+
(1) Na prevents water loss from body (2) NaCI function as regulatory material
(3) NaCI produces energy (4) NaCI is antibacterial
42. A nutrient which is used to build protoplasm is- [RPMT 2001]
(1) Fat (2) Protein (3) Carbohydrate (4) Calcium
43. Two elements needed for building healthy teeth and bones are: [RPMT 2001]
(1) iron and calcium (2) phosphorous and iron
(3) calcium and phosphorous (4) CO2 and H2O
44. If all the peptide bonds of protein are broken, then the remaining part is : [RPMT 2002]
(1) amide (2) oligosaccharide (3) polypeptide (4) amino acid
45. Which of the following is a disaccharide? [RPMT 2002]
(1) Glucose (2) Fructose (3) Sucrose (4) Galactose
46. The chemical formula of starch is : [RPMT 2002]
(1) (C6H10O5)n (2) (C6H12O6)n (3) C12H12O11 (4) CH3COOH
47. Which elements is located at the centre of the porphyrin ring in chlorophyll- [CMEET 2003]
(1) Calcium (2) Magnesium (3) Potassium (4) Mangnese
48. In protoplasm fat store is in the form of- [RPMT 2004]
(1) Polypeptide (2) Triglyceride (3) Polysaccharide (4) Nucleosides
49. Antibody is formed by- [RPMT 2004]
(1) Protein (2) Carbohydrate (3) Nucleic acid (4) Lipid
50. Major cause of anaemia- [BHU 2004]
(1) Deficiency of Ca (2) Deficiency of Fe (3) Deficiency of Na (4) Deficiency of Mg
51. Deficiency of copper causes- [Manipal 2004]
(1) Pellagra (2) Anemia and damage to CNS
(3) Influenza (4) Xerophthalmia
52. Cytochromes are- [NDA2004]
(1) Riboflavin nucleotides (2) Pyrimidine nucleotides
(3) Iron porphyrin proteins (4) Flavoproteins
53. Starch and cellulose are the compounds made up of many units of [CPMT 1988, 89, 93, 2009]
(1) Simple sugar (2) Fatty acid (3) Glycerol (4) Amino acid
54. Which of the following is the characteristic of plants [MP PMT 2003]
(1) Glucose and cellulose (2) Pyruvic acid and glucose
(3) Cellulose and starch (4) Starch and pyruvic acid
55. Inulin found in plant cell is a [Orissa PMT 2002]
(1) Lipid (2) Protein (3) Polysaccharide (4) Vitamin
56. Which of the following structure is not common in all protein [Bihar CECE 2006]
(1) Primary structure (2) Secondary structure
(3) Tertiary structure (4) Quarternary structure
57. Oval shaped and eccentric starch particles are found in [RPMT 1995]
(1) Wheat (2) Maize (3) Potato (4) Rice
58. What are the most diversed molecules in the cell [MP PMT 2000]
(1) Lipids (2) Proteins (3) Carbohydrates (4) Mineral salts

NEET_BIOMOLECULES-1 - 36
59. No cell could live without [MP PMT 1997]
(1) Phytochrome (2) Enzymes (3) Chloroplasts (4) Protein
60. -helical model of protein was discovered by [BVP 2000; MHCET 2001]
(1) Pauling and Correy (2) Watson (3) Morgan (4) Berzilius
61. Aleurone grains are [BVP2003]
(1) Enzymes (2) Carbohydrates (3) Protein (4) Fat
62. High content of lysine is present in [MHCET 2003]
(1) Wheat (2) Apple (3) Maize (4) Banana
63. Arachidonic acid is [MHCET 2003]
(1) Non-essential fatty acid (2) Essential fatty acid
(3) Polyunsaturated fatty acid (4) Both (2) and (3)
64. Maltose consists of which one of the following [Manipal 2005]
(1) - glucose and - galactose (2) - glucose and - fructose
(3) - sucrose nad - glucose (4) Glucose and glucose
65. Paraffin wax is [BHU 2006]
(1) Ester (2) Acid (3) Monohydric alcohol (4) Cholesterol
66. Match the items in column I with items in column II and choose the correct answer
[Kerala PMT 2006]

Column I Column II
A Triglyceride 1 Animal hormones
B Membrane lipid 2 Feathers and leaves
C Steroid 3 Phospolipids
D W ax 4 Fat stored in form of droplets

(1) A - 4, B - 3, C - 1, D - 2 (2) A - 2, B - 3, C - 4, D - 1
(3) A - 3, B - 4, C - 1, D - 2 (4) A - 4, B - 1, C - 2, D - 3
67. Given below is the chemical formula of

[Kerala PMT 2007]

(1) Palmitic acid (2) Stearic acid (3) Glycerol (4) Galactose
68. Select the wrong statement [Kerala PMT 2007]
(1) The building blocks of lipids are amino acids
(2) Majority of enzymes contain a non-protein part called the prosthetic group
(3) The thylakoids are arranged one above the other like a stack of coins forming a granum
(4) Crossing-over occurs at pachytene stage of meiosis I
69. What does the following equation denote? Amino acid + ATP Aminoacyl AMP + PP
(1) Elongation of chain (2) Chain termination [OPMT2007]
(3) Activation of amino acid (4) None of these
70. Which of the following fats is least harmful for heart [OPMT2007]
(1) Saturated fat (2) Cholesterol (3) Polyunsaturated fat (4) Oils

NEET_BIOMOLECULES-1 - 37
71. Quarternary structure of protein [WBJEE 2008]
(1) Consists of four subunits
(2) May be either or
(3) Is unrelated to two function of the protein
(4) Is dictated by the primary structures of the individual subunits
72. During strenuos exercise, glucose is converted into (BHU mains - 2008)
(1) Starch (2) Glycogen (3) Lactic acid (4) Pyruvic acid
73. The "repeating unit" of glycogen is [WBJEE 2009]
(1) Fructose (2) Mannose (3) Glucose (4) Galactose
74. Starch is polymer of (UP. CPMT - 2009)
(1) Glucose (2) Sucrose (3) Maltose (4) Fructose
75. Table sugar is (UP. CPMT - 2009)
(1) Sucrose (2) Glucose (3) Fructose (4) Lactose
76. Which of the following is not an unsaturated fatty acid? (UP. CPMT - 2009)
(1) Stearic acid (2) Linoleic acid (3) Linolenic acid (4) Oleic acid
77. Prostaglandins are (UPCPMT - 2009)
(1) Amino acid (2) Fatty acid (3) Carbohydrate (4) Steroid
78. Protein which plays a significant role in ageing is (UPCPMT - 2009)
(1) Collagen (2) Elastin (3) Actin (4) Myosin

NEET_BIOMOLECULES-1 - 38
BOARD LEVEL EXERCISE : HINT & SOLUTIONS

1. Those molecules which have molecular weight less than 1000 dalton known as microbiomolecule.
Ex. Amino acid, Glucose etc.
2. Storage food of animal body is glycogen and storage food of plant body is starch.
3. Macromolecules which are found in acid insoluble fraction protein, nucleic acid and polysaccharides.
4. The name of various polysaccharides are cellulose , glycogen, chitin, inulin, starch etc.
5. Zwitter ion

6. Inulin - Fructose
Protein - Amino acid
Lipid - Fatty acid & Glycerol
7. All the carbon compounds that we get from living tissues can be called biomolecules.
8. Primary metabolites - Carbohydrate, amino acid, fatty acid, nitrogenous base, cholesterol.
Secondary metabolites - Pigment , toxin, terpenoid, drugs, alkaloids.
9. See pg. no. 5

10. See pg. no. 15

11. See pg. no. 10

12. See pg. no. 13

13. See pg. no. 17, 18

14. See pg. no. 11

15. See pg. no. 10

EXERCISE - 1
1. (4) 2. (3) 3. (4) 4. (3) 5. (4) 6. (2) 7. (2)
8. (4) 9. (1) 10. (1) 11. (1) 12. (4) 13. (4) 14. (4)
15. (3) 16. (2) 17. (3) 18. (4) 19. (3) 20. (1) 21. (3)
22. (3) 23. (1) 24. (2) 25. (4) 26. (3) 27. (2) 28. (2)
29. (1) 30. (1) 31. (2) 32. (3) 33. (2) 34. (1) 35. (4)
36. (1) 37. (3) 38. (4) 39. (2) 40. (4) 41. (4) 42. (2)
43. (2) 44. (1) 45. (1) 46. (4) 47. (1) 48. (2) 49. (1)
50. (4) 51. (3) 52. (3) 53. (1) 54. (3) 55. (1) 56. (1)
57. (1) 58. (1) 59. (2) 60. (3) 61. (1) 62. (2) 63. (1)
64. (1) 65. (4) 66. (2) 67. (3) 68. (4) 69. (3) 70. (2)
71. (4) 72. (3) 73. (3) 74. (1) 75. (3) 76. (1) 77. (2)
78. (4) 79. (1) 80. (3) 81. (1) 82. (4) 83. (3) 84. (1)
85. (2) 86. (3) 87. (2) 88. (2) 89. (2) 90. (4) 91. (4)
92. (2) 93. (4) 94. (4) 95. (3) 96. (1) 97. (3) 98. (4)
99. (2)

NEET_BIOMOLECULES-1 - 39
EXERCISE - 2
1. (2) 2. (3) 3. (3) 4. (2) 5. (3) 6. (4) 7. (3)
8. (4) 9. (1) 10. (2) 11. (1) 12. (2)

EXERCISE - 3
1. (3) 2. (2) 3. (3) 4. (1) 5. (1) 6. (2) 7. (3)
8. (2) 9. (2) 10. (3) 11. (2)

EXERCISE - 4
Level - I
1. (1) 2. (2) 3. (4) 4. (2) 5. (4) 6. (2) 7. (1)
8. (1) 9. (3) 10. (1) 11. (2) 12. (1) 13. (2) 14. (2)
15. (4) 16. (3) 17. (3) 18. (3) 19. (1) 20. (4) 21. (2)

Level - II
22. (1) 23. (2) 24. (1) 25. (2) 26. (3) 27. (1) 28. (3)
29. (4) 30. (3) 31. (1) 32. (1) 33. (4) 34. (1) 35. (1)
36. (2) 37. (3) 38. (4) 39. (4) 40. (2) 41. (1) 42. (2)
43. (3) 44. (4) 45. (3) 46. (1) 47. (2) 48. (2) 49. (1)
50. (2) 51. (2) 52. (3) 53. (1) 54. (3) 55. (3) 56. (4)
57. (3) 58. (2) 59. (4) 60. (1) 61. (3) 62. (1) 63. (2)
64. (4) 65. (1) 66. (1) 67. (1) 68. (1) 69. (3) 70. (3)
71. (4) 72. (3) 73. (3) 74. (1) 75. (1) 76. (1) 77. (2)
78. (1)

NEET_BIOMOLECULES-1 - 40
Biomolecules - 2

"The other type of macromolecule that one would find in the acid insoluble fraction of any living tissue is
the nucleic acid.
These are polynucleotides. Together with polysaccharides and polypeptides these comprise the true
macromolecular fraction of any living tissue or cell.
For nucleic acids, the building block is a nucleotide. A nucleotide has three chemically distinct
components. One is a heterocyclic compound, the second is a monosaccharide and the third a phosphoric
acid or phosphate.
It is of two types (A) DNA (B) RNA

(A) DNA (Deoxyribonucleic Acid)


Term was given by Zacharis, which is found in the cells of all living organisms except plant viruses,where
RNA forms the genetic material and DNA is absent.

In bacteriophages and viruses there is a single molecule of DNA, which remains coiled and is enclosed
in the protein coat.

In bacteria, mitochondria, plastids and other prokaryotes, DNA is circular and lies naked in the cyto-
plasm

In eukaryotes it is found in nucleus and known as carrier of genetic information and capable of self
replication.

1. Chemical Composition

The chemical analysis has shown that DNA is composed of three different types of compound.

(i) Sugar molecule : Levene identified a five carbon sugar, ribose in nucleic acid in 1910. It is represented by
a pentose sugar the deoxyribose or 2-deoxyribose which derived from ribose due to the deletion of oxygen
from the second carbon.

(ii) Phosphoric acid : H3PO4 that makes DNA acidic in nature.

(iii) Nitrogeneous base : Kossel demonstrated the presence of two pyrimidines (cytosine and thymine)
and two purines (adenine and guanine) in DNA and he was awarded Nobel Prize in 1910. These are
nitrogen containing ring compound. Which classified into two groups:

(a) Purines : Two ring compound namely as Adenine and Guanine.


(b) Pyrimidine : One ring compound included Cytosine and Thymine. In RNA Uracil is present instead of
Thymine.
Nucleosides : Nucleosides are formed by a purine or pyrimidine nitrogenous base and pentose sugar. DNA
nucleosides are known as deoxyribosenucleosides.
Nucleotides : In a nucleotide, purine or pyrimidine nitrogenous base is joined by deoxyribose pentose sugar
(D), which is further linked with phosphate (P) group to form nucleotides.

NEET_Biomolecules-2 - 41
Nitrogenous base Nucleoside Nucleotide

Fig. : Some structures related to biomolecules


2. Watson and Crick’s model of DNA
In 1953 James Watson and Francis Crick suggested that in a DNA molecule there are two such polynucle-
otide chains arranged antiparallal or in opposite directions i.e., one polynucleotide chain runs in 5’ to 3’
direction, the other in 3’to 5’ direction. It means the 3’ end of one chain lies beside the 5’ end of other in right
handed manner.
Important features
Nucleic acids exhibit a wide variety of secondary structures. For example, one of the secondary struc-
tures exhibited by DNA is the famous Watson-Crick model. This model says that DNAexists as a double
helix.

NEET_Biomolecules-2 - 42
The double helix comprises of two polynucleotide chains.
The two strands (polynucleotide chains) of double helix are anti-parallel due to phosphodiester bond.
Each polynucleotide chain has a sugar-phosphate ‘backbone’ with nitrogeneous bases directed inside
the helix.
The nitrogenous bases of two antiparallel polynucleotide strands are linked through hydrogen bonds.
There are two hydrogen bonds between A and T, and three between G and C. The hydrogen bonds are
the only attractive forces between the two polynucleotides of double helix. These serve to hold the
structure together.
The two polynucleotides in a double helix are complementary. The sequence of nitrogenous bases in
one determines the sequence of the nitrogenous bases in the other. Complementary base pairing is of
fundamental importance in molecular genetics.

20 A°

Shallow
groove

3.4 A°

Deep groove
10 A°

Major axis
Shallow
groove

NEET_Biomolecules-2 - 43
Erwin Chargaff (1950) made quantitative analysis of DNA and proposed “base equivalence rule”. Start-
A G A T
ing molar concentration of A = T & G C or =1 and which is constant for a species. Sugar
C T G C
deoxyribose and phosphate occur in equimolar proportion.
Ten base pairs occur per turn of helix (abbreviated 10bp). The spacing between adjacent base pairs is
3.4Å. The helix is 20Å (19.8Å) in diameter and DNA molecule found 360 o in a clockwise.

(B) RNA (Ribonucleic Acid)


1. Structure of RNA
More commonly RNA is a single stranded structure consisting of an unbranched polynucleotide chain, but
it is often folded back on itself forming helices. DNA is a double stranded structure and its two polynucleotide
chains are bounded spirally around a main axis. It is made up by :
(1) Sugar : Ribose
(2) Phosphate : In the form of H3PO4.
(3) Nitrogenous base : Two types:
(a) Purine,
(b) Pyrimidine
(a) Purine is further divided into Adenine and Guanine.
(b) Pyrimidine divided into Cytosine and Uracil.
2. Types of RNA
(a) Genetic RNA : Which established by Conrat. In most of the plant viruses, some animal viruses and in
many bacteriophages DNA is not found and RNA acts as hereditary material. This RNA may be single
stranded or double stranded.
(b) Nongenetic RNA : In the all other organisms where DNA is the hereditary material, different types of RNA
are nongenetic. The nongenetic RNA is synthesized from DNA template.
In general, three types of RNAs have been distinguished :
1. Messenger RNA (mRNA) :
Name mRNA was given by Jacob and Monod (1961) on the basis of his informative work.
It forms 5% of total RNA.
It is complementary strand to DNA and carries genetic information in cytoplasm for the synthesis of
proteins.
It acts as a template for protein synthesis and has a short life span.
2. Ribosomal RNA (rRNA) :
rRNA constitutes redundant nature upto 80% of total RNA of the cell.
It occurs in ribosomes, which are nucleoprotein molecules.
Inside the ribosomes of eukaryotic cells rRNA occurs in the form of the particles of four different
dimensions. These are designated 28S, 18S, 5.8S and 5S. The 28S, 5.85S and 5S molecules occur in
large subunit (60S subunit) of ribosome, whereas 18S molecules is present in the small subunit (40S
subunit) of ribosome.
In prokaryotic cells there are only 23S, 16S and 5S rRNA are found. Which are synthesized in Nucleolus
/ SAT region.
3. Transfer RNA (tRNA) :
It is about 10-15% of RNA of the cell.
tRNA molecules have been variously termed as soluble RNA or supernatant RNA or adapter RNA.
tRNA molecules are smallest, containing 75 to 80 nucleotides.
The transfer RNA is a family of about 60 small sized ribonucleic acids which can recognize the codons
of mRNA and exhibit high affinity for 20 activated amino acids,

NEET_Biomolecules-2 - 44
2.1 DYNAMIC STATE OF BODY CONSTITUENTS - CONCEPT OF METABOLISM :
Basically livingorganisms, like a simple bacterial cell, a protozoan, a plant or an animal, contain thou-
sands of organic compounds.
These compounds or biomolecules are present in certain concentrations (expressed as mole/cell or
mole/Iitre etc.).
All these biomolecules have a turn over. This means that they are constantly being changed into some
other biomolecules and also made from some other biomolecules. This breaking and making is through
chemical reactions constantly occuring in living organisms. Together all these chemical reactions are
called metabolism.
Each of the metabolic reactions results in the transformation of biomolecules. A few examples for such
metabolic transformations are: removal of CO2 from amino acids making an amino acid into an amine,
removal of amino group in a nucleotide base; hydrolysis of a glycosidic bond in a disaccharide, etc. In
other words, metabolites are converted into each other in a series of linked reactions called metabolic
pathways. These metabolic pathways are similar to the automobile traffic in a city.These pathways are
either linear or circular.
These pathways criss- cross each other, i.e., there are traffic junctions. Flow of metabolites through
metabolic pathway has a definite rate and direction like automobile traffic.
This metabolite flow is called the dynamic state of body constituents. Most important is that this interlinked
metabolic traffic is very smooth and without a single reported mishap for healthy conditions.
Another feature of these metabolic reactions is that every chemical reaction is a catalysed reaction.
There is no uncatalysed metabolic conversion in living systems. Even CO2 dissolving in water, a physical
process, is a catalysed reaction in living systems.
The catalysts which hasten the rate of a given metabolic conversation are also proteins. These
proteins with catalytic power are named enzymes.
2.2 METABOLIC BASIS FOR LIVING :
Metabolic pathways can lead to a more complex structure from a simpler structure (forexample, acetic
acid becomes cholesterol) or lead to a simpler structure from a complex structure (for example, glucose
becomes lactic acid in our skeletal muscle).
The former cases are called biosynthetic pathways or anabolic pathways The latter constitute degradation
and hence are called catabolic pathways.
Anabolic pathways, as expected, consume energy. Assembly of a protein from amino acids requires
energy input.
On the other hand, catabolic pathways lead to the release of energy. Forexample,when glucose is
degraded to lactic acid in our skeletal muscle, energy is liberated.This metabolic pathway from glucose
to lactic acid which occurs in 10 metabolic steps is called glycolysis.
Living organisms have learnt to trap this energy liberated during degradation and store it in the form of
chemical bonds. As and when needed, this bond energy is utilised for biosynthetic, osmotic and
mechanical work that we perform.
The most important form of energy currency in living systems is the bond energy in a chemical called
adenosine triphosphate (ATP).
2.3 THE LIVING STATE :
Basically tens and thousands of chemical compounds in a living organism, otherwise called metabolites,
or biomolecules, are present at concentrations characteristic of each of them. For example, the blood
concentration of glucose in a normal healthy individual is 4.5-5.0 mM, while that of hormones would be
nanograms/ mL. In animal tissue carbohydrate, protein, lipid, amino acid etc. are called primary
metabolite and rubber, antibiotic, flavinoid, pigments etc. are called secondary metabolite.

NEET_Biomolecules-2 - 45
The most important fact of biological systems is that all living organisms exist in a steady-state
characterised by concentrations of each. of these biomolecules. These biomolecules are in a metabolic
flux.
Any chemical of physical process moves spontaneously to equilibrium.
The steady state is a non-equilibirium state.
One should remember from physics that systems at equilibrium cannot perform work. As living
organisms work continuously, they cannot afford to reach equilibrium.
Hence the living state is a non-equilibrium steady-state to be able to perform work.
Living process is a constant effort to prevent falling into equilibrium. This is achieved by energy
input.
Metabolism provides a mechanism for the production of energy. Hence the living state and
metabolism are synonymous. Without metabolism there cannot be a living state.

When we try to define ‘living’, we conventionally look for distinctive characteristics exhibited by living
organisms.
Growth, reproduction, ability to sense environment and mount a suitable response come to our
mind immediately as unique features of living organisms.
One can add a few more features like metabolism, ability to self-replicate, self-organise, interact
and emergence to this list. Let us try to understand each of these.
3.1 GROWTH :
All living organisms grow.
Increase in mass and increase in number of individuals are twin characteristics of growth.
A multicellular organism grows by cell division.
In plants, this growth by cell division occurs continuously throughout their life span. In animals, this
growth is seen only up to a certain age.
However, cell division occurs in certain tissues to replace lost cells. Unicellular organisms also grow by
cell division.
In majority of higher animals and plants, growth and reproduction are mutually exclusive events.
One must remember that increase in body mass is considered as growth.
Non-living objects also grow if we take increase in body mass as a criterion for growth.
Mountains, boulders and sand mounds do grow. However, this kind of growth exhibited by non-
living objects is by accumulation of material on the surface.
In living organisms, growth is from inside. Growth, therefore, cannot be taken as a defining
property of living organisms.
Conditions under which it can be observed in all living organisms have to be explained and then we
understand that it is a characteristic of living systems.
A dead organism does not grow.
3.2 REPRODUCTION :
Reproduction, likewise, is a characteristic of living organisms.
In multicellular organisms, reproduction refers to the production of progeny possessing features more or
less similar to those of parents. Invariably and implicitly we refer to sexual reproduction.
Organisms reproduce by asexual means also.
Fungi multiply and spread easily due to the millions of asexual spores they produce.
In lower organisms like yeast and hydra, we observe budding. In Planaria (flat worms), we observe true
regeneration, i.e., a fragmented organism regenerates the lost part of its body and becomes, a new
organism.
The fungi, the filamentous algae, the protonema of mosses, all easily multiply by fragmentation.
When it comes to unicellular organisms like bacteria, unicellular algae or Amoeba, reproduction
is synonymous with growth, i.e., increase in number of cells.

NEET_Biomolecules-2 - 46
3.3 METABOLISM
Another characteristic of life is metabolism.
All living organisms are made of chemicals. These chemicals, small and big, belonging to various
classes, sizes, functions, etc., are constantly being made and changed into some other biomolecules.
These conversions are chemical reactions or metabolic reactions.
There are thousands of metabolic reactions occurring simultaneously inside all living organisms, be they
unicellular or multicellular.
All plants, animals, fungi and microbes exhibit metabolism.
The sum total of all the chemical reactions occurring in our body is metabolism.
No non-living object exhibits metabolism.
Metabolic reactions can be demonstrated outside the body in cell-free systems. An isolated
metabolic reaction(s) outside the body of an organism, performed in a test tube is neither living
nor non-living.
Hence, while metabolism is a defining feature of all living organisms without exception, isolated
metabolic reactions in vitro are not living things but surely living reactions.
Hence, cellular organisation of the body is the defining feature of ife forms.
3.4 SENSES
Perhaps, the most obvious and technically complicated feature of all iving organisms is this ability to
sense their surroundings or environment and respond to these environmental stimuli which could be
physical Chemical or biological.
We sense our environment through our sense Organs.
Plants respond to external factors like light, water, temperature, other organisms, pollutants, etc. All
organisms, from the prokaryotes to the most complex eukaryotes can sense and respond to environmental
use.
Photoperiod affects reproduction in seasonal breeders, both plants and animals.
All organisms handle chemicals entering their bodies.
All organisms therefore, are ‘aware’ of their surroundings. Human being is he only organism who is
aware of himself, i.e., has self-consciousness.
Consciousness therefore, becomes the defining property of living organisms.
When it comes to human beings, it is all the more difficult to define the living state.
We observe patients lying in coma in hospitals virtually supported by machines which replace heart and
lungs. The patient is otherwise brain-dead. The patient has no self-consciousness. Are such patients
who never come back to normal life, living or non-living?

In higher classes, you will come to know that all living phenomena are due to underlying interactions.
Properties of tissues are not present n the constituent cells but arise as a result of interactions among
the constituent cells. Similarly, properties of cellular organelles are not present in the molecular constituents
of the organelle but arise as a result of nteractions among the molecular components comprising the
organelle. These interactions result in emergent properties at a higher level of organisation. This
phenomenon is true in the hierarchy of organisational complexity at all levels. Therefore, we can say
that living organisms are self-replicating, evolving and self-regulating interactive systems capable of
responding to external stimuli.
Biology is the story of life on earth. Biology is the story of evolution of living organisms on earth. All living
organisms – present, past and future, are linked to one another by the sharing of the common genetic
material, but to varying degrees.

NEET_Biomolecules-2 - 47
4.1 History of cellular enzymes :
Enzymes (Gk. en = in; zyme = yeast) are proteinaceous substances which are capable of catalysing
chemical reactions of biological origins without themselves undergoing any change.
Enzymes are biocatalysts. An enzyme may be defined as “a protein that enhances the rate of bio-
chemical reactions but does not affect the nature of final product”.
They are produced by living cells only.
Enzymes are also called ‘biological middle man’.
The study of the composition and function of the enzyme is known as enzymology.
The term enzyme (meaning in yeast) was used by Willy Kuhne (1878), while working on fermentation.
At that time living cells of yeast were thought to be essential for fermentation of sugar.
Edward Buchner (1897), a German chemist proved that extract zymase, obtained from yeast cells, has
the power of fermenting sugar (alcoholic fermentation).
There are some nucleic acids that behave like enzymes. These are called ribozymes. Ex : RNA
enzymes (RNase)
Northrop and Kunitz prepared crystals of pepsin, trypsin and chymotrypsin
Arber and Nathans got noble prize in 1978 for the discovery of restriction endonucleases which break
both strands of DNA at specific sites and produce sticky ends. These enzymes are used as microscissors
in genetic engineering.

Do You Know ?
Zymogen :- These are precursor of enzymes are known as zymogens

Examples -

(1) Pepsinogen pH 2 Pepsin

(2) Prorennin Pepsin Rennin

(3) Trypsinogen Enterokina se Trypsin

(4) Chymotrypsinogen Tryp sin Chymotrypsin

4.2 Types of enzymes


Two types of enzymes are -
(i) Simple enzyme-Made up of only protein. Ex.- Urease, Amylase, Trypsin, Pepsin
(ii) Conjugated enzyme- Made up of protein and nonprotein part. Non protein part is called cofactor
Protein part is called Apoenzyme. Both Combinely called Holoenzyme.
Holo enzyme = Apoenzyme + co-factor
Activity of enzyme is due to co-factor, which can be separated by dialysis. co-factor is small,
heat stable and may be organic or inorganic in nature.
Three types of cofactors may be identified. Prosthetic group, coenzyme and metal ions.
(i) Prosthetic group : Prosthetic groups are organic compounds distinguished from other
cofactors in that they are permanently bound to the apoenzyme, e.g., in peroxisomal enzymes
peroxidase and catalase which catalyzes breakdown of hydrogen peroxide to water and oxy-
gen. haem is the prosthetic group and it is a part of the active site of the enzyme.
(ii) Coenzymes : Lipmann discovered coenzymes. Coenzymes are also organic compounds
but their association with the apoenzyme is transient, usually occurring only during the course
of catalysis. In general coenzymes not only assist enzymes in the cleavage of the substrate but
also serve as temporary acceptor for one of the product of the reaction. The essential chemical
component of many coenzymes are vitamins, e.g., coenzyme nicotinamide adenine dinucle-

NEET_Biomolecules-2 - 48
otide (NAD), nicotinamide adenine dinucleotide phosphate (NADP) contains the vitamin nia-
cin.
(iii) Metal ions : A number of enzymes require metal ions for their activity. The metal ions form
coordination bonds with specific side chains at the active site and at the same time form one or
more coordination bonds with the substrate. The latter assist in the polarization of substrate
bonds to be cleaved by the enzyme. The common metal ions are Zn++, Cu++, Mg++. Inorganic
part of enzyme acts as prosthetic group in few enzymes they are called activators. These
activators are generally metals. Hence these enzymes are called Metalloenzyme such as :

Enzymes activators
Activators Enzymes
Iron (Fe) Acotinase, Catalase and Cytochrome oxidase
Zinc (Zn) Dehydrogenase, Carbonic anhydrase
Copper (Cu) Tyrosinase, Cytochrome oxidase
Magnesium (Mg) Haxokinase, Phosphotransferase
Manganese (Mn) Peptidase, Decarboxylase
Molybdenum (Mo) Nitrate reductase
Nickel (Ni) Urease
Boron (B) Enolase

4.3 Classification and Nomenclature of enzymes :


Thousands of enzymes have been discovered, isolated and studied. Most of these enzymes have been
classified into different groups based on the type of reactions they catalyse.
Enzymes are divided into 6 classes each with 4-13 subclasses and named accordingly by a four-digit
number.
The first digit denotes the class, the second sub-class, the third sub-sub-class and the fourth one is for
the particular enzyme name. Thus, E.C. 2.7.1.1 denotes class 2 (Transferases)-subclass 7 (transfer of
phosphate) sub-sub-class 1 (an alcohol functions as phosphate acceptor). The 4th digit indicates hexoki-
nase.
(i) Oxidoreductases/dehydrogenases : These enzymes catalyse oxidation reduction reactions,
usually involving the transfer of hydrogen atoms or ions from one molecule to another.
S reduced + S’ oxidised S oxidised + S’ reduced.
(ii) Transferases : These enzyme catalyse the transfer of a specific group (e.g., amino, methyl, acyl,
phosphate) from one kind of molecule to another. G (other than hydrogen) between a pair of sub-
strate S and S’.
e.g. :- S - G + S’ S + S’ - G
Ex. Phosphotransferase, Peptidyl transferase etc.
(iii) Hydrolases : These enzyme catalyse the hydrolysis of organic foods i.e., the breakdown of
large molecules by addition of water. Most of the hydrolysing (digestive) enzymes are located in
lysosomes. e.g., all digestive enzymes such as lipases (digest the stored food material of castor
seeds).
(iv) Lyases : These enzymes catalyse the breakage of specific covalent bonds and removal of
groups without hydrolysis e.g., fumerases, carboxylases, aminases, histidine decarboxylase that
splits C–C-bond of histidine, forming CO2 and histamine.
X Y
| |
C–C X Y C C
(v) Isomerases : These enzymes catalyse the rearrangement molecular structure to form isomers.
e.g., phosphohexose isomerase (phosphoglucomutase) act on glucose 6-phosphate to form fructose
6-phosphate (both C6 compounds)

NEET_Biomolecules-2 - 49
(vi) Ligases or Synthetases : These enzymes form bonds and join two molecules together, using
energy supplied from the breakdown of ATP, e.g., DNA ligase is used to repair breaks in DNA
molecules.

Nomenclature and Classification


Dauclax, (1883) introduced the nomenclature of enzyme. Usually enzyme names end in suffix-ase to the
name of substrate e.g., Lactase acts on lactose, maltase act on maltose, amylase on amylose, sucrase on
sucrose, protease on proteins, lipase on lipids and cellulase on cellulose. Sometimes arbitrary names are
also popular e.g., Pepsin, Trypsin and Ptylin etc. Few names have been assigned as the basis of the
source from which they are extracted e.g., Papain from papaya, bromelain from pineapple (family
Bromeliaceae). Enzymes can also be named by adding suffix–ase to the nature of chemical reaction also
e.g., Oxidase, dehydrogenase, catalase, DNA polymerase.
Modern names are given after chemical action. They are more systamatic, informative but slightly longer.
e.g., ATP : D-glucose phosphotransferase.
Common simpler names used at the place of systematic names called trivial names.
According to older classification : The older classification of enzymes is based on the basis of reactions
which they catalyse. Many earlier authors have classified enzymes into two groups :
(1) Hydrolysing enzyme : The hydrolysing enzymes of hydrolases catalyse reactions in which complex
organic compounds are broken into simpler compounds with the addition of water. Depending upon the
substrate hydrolysing enzymes are :
Carbohydrases : Most of the polysaccharides, disaccharides or small oligosaccharides are hydrolysed to
simpler compounds, e.g., hexoses or pentoses under the influence of these enzymes.
Lactase on lactose to form glucose to galactose, sucrase/invertase on sucrose to form glucose and fruc-
tose, amylase or diastase on starch to form maltose, maltase on maltose to form glucose, cellulase on
cellulose to produce glucose.
Easterases : These enzymes catalyse the hydrolysis of substances containing easter linkage, e.g., fat,
pectin, etc. into an alcoholic and an acidic compound.
Proteolytic enzymes : The hydrolysis of proteins into peptones, polypeptides and amino acids is catalysed
by these enzymes

Amidases : They hydrolyse amides into ammonia and acids.


(2) Desmolysing enzymes : Most of the desmolysing enzymes are the enzymes of respiration e.g.,
oxidases, dehydrogenases, (concerned with transfer of electrons), transaminases carboxylases etc.

4.4 Mechanism of enzyme action :


Energy is required to bring the inert molecules into the activated state. The amount of energy required to
raise the energy of molecules at which chemical reaction can occur is called activation energy. Enzymes
act by decreasing the activation energy so that the number of activated molecules is increased at lower
energy levels. If the activation energy required for the formation of the enzyme-substrate complex is low,
many more molecules can participate in the reaction than would be the case if the enzyme were absent.

NEET_Biomolecules-2 - 50
4.5 Nature of Enzyme Action
Each enzyme (E)has a substrate (S)binding site in its molecule so that a highly reactive enzyme-substrate
complex (ES) is produced. This complex is short-lived and dissociates into its product (P) and the un-
changed enzyme with an intermediate formation of the enzyme-product complex (EP). - The formation of the
ES complex is essential for catalysis.

The catalytic cycle of an enzyme action can be described in the following steps:
1. First, the substrate binds to the active site of the enzyme, fitting into the active site.
2. The binding of the substrate induces the enzyme to alter its shape, fitting more tightly around the sub-
strate.
3. The active site of the enzyme, now in close proximity of the substrate breaks the chemical bonds of the
substrate and the new enzyme- product complex is formed.
4. The enzyme releases the products of the reaction and the free enzyme is ready to bind to another
molecule of the substrate and run through the catalytic cycle once again.
There are two theories to explain the mode of action of enzymes.
Lock and Key hypothesis : The hypothesis was put forward by Emil Fisher (1894). According to this
hypothesis the enzyme and its substrate have a complementary shape. The specific substrate molecules
are bound to a specific site of the enzyme molecule.
The theory can be explained easily by the fact that a particular lock can be opened by a particular key
specially designed to open it. Similarly enzymes have specific sites where a particular substrate can only be
attached. The lock and key model accounts for enzyme specificity.

Induced fit hypothesis : This hypothesis was proposed by Daniel, E. Koshland (1959).
According to this view, active site is not rigid but static and it has two groups – buttressing group and
catalytic group. Initially substrate bind to the buttressing group which induces the catalytic group to fit the
substrate and catalytic group weakes the bonds of reactant or substrate by electrophilic and nucleophilic
forces.

NEET_Biomolecules-2 - 51
Site of enzyme action
All enzymes are produced in the living cells. About 3,000 enzymes have recorded. These are of two types
with regard to the site where they act as :
Intracellular enzymes : Most of the enzymes remain and function inside the cells, They are called the
intracellular enzymes or endoenzymes. Some of these enzymes are found in cytoplasmic matrix. Certain
enzymes are bound to ribosomes, mitochondria and chloroplast etc.
Extracellular enzymes : Certain enzymes leave the cells and function outside them. They are called the
extracellular enzymes or exoenzymes. They mainly include the digestive enzymes. e.g., salivary amylase,
gastric pepsin, lysozyme present in tears and nasal secretion.
Rennet tablets with enzyme renin from calf’s stomach are widely used to coagulate protein caseinogen for
cheese (casein) formation.

4.6 Properties of enzymes :


(1) Chemical reactions
Chemical compounds undergo two types of changes. A physical change simply refers to a change in
shape without breaking of bonds. This is a physical process. Another physical process is a change in state
of matter when ice melts into water, or when water becomes a vapour. These are physical processes.
However, when bonds are broken and new bonds are formed during transformation, this will be called a
chemical reaction. For example
Ba(OH)2 + H2 SO4 BaSO4 + 2H2O
is an inorganic chemical reaction. Similarly, hydrolysis of starch into glucose is an organic chemical
reaction. Rate of a physical or chemical process refers to the amount of product formed per unit time. It
P
can be expressed as rate =
t
Rate can also be called velocity if the direction is specified. Rates of physical and chemical processes are
influenced by temperature among other factors, A general rule of thumb is that rate doubles or decreases
by half for every 10ºC change in either direction. Catalysed reactions proceed at rates vastly higher than
that of uncatalysed ones. When enzyme catalysed reactions are observed, the rate would be vastly higher
than the same but uncatalysed reaction. For example.

CO2 + H 2O Carbonic anhydrase H2CO3



Carbon dioxide water carbonic acid
In the absence of any enzyme this reaction is very slow, with about 200 molecules of H2CO3 being formed
in an hour. However, by using the enzyme present within the cytoplasm called carbonic anhydrase, the
reaction speeds dramatically with about 600,000 molecules being formed every second. The enzyme has
accelerated the reaction rate by about 10 million times. The power of enzymes is incredible indeed
There are thousands of types of enzymes each catalysing a unique chemical of metabolic reaction. A

NEET_Biomolecules-2 - 52
multistep chemical reaction, when each of the steps is catalysed by the same enzyme complex or different
enzymes, is called a metabolic pathway. For example.
Glucose 2 Pyruvic acid
C6H12O6 + O2 2C3H4O3 + 2H2O

(2) Colloidal nature : All enzymes are colloidal in nature and thus provide large surface area for reaction
to take place. They posses extremely low rates of diffusion and form colloidal system in water.

(3) Catalytic properties : Enzymes are active in extremely small amounts, e.g., one molecule of invertase
can effectively hydrolyze 1,000,000 times its own weight of sucrose. One molecule of catalase is able to
catalyze conversion of 5,000,000 molecules of hydrogen peroxide.

(4) High efficiency : The effectiveness of an enzymatic reaction is expressed in terms of its turn over
number or catalytic centre activity means number of substrate molecules on which one enzymes molecules
acts in one minute.
(5) Molecular weight : Enzymatic proteins are substances of high molecular weight. Bacterial ferredoxin
one of the smaller enzymes has molecular weight of 6,000, where as pyruvic dehydrogenase one of the
largest-has a molecular weight of 4600000.

(6) Specificity of enzyme : Most of the enzymes are highly specific in their action. A single enzyme will
generally catalyze only a single substrate or a group of closely related substrates. The active site possess
a particular binding site which complexes only with specific substrate. Thus, only a suitable substrate fulfils
the requirements of active site and closely fixes with it.
(7) Reversibility of reaction : The enzyme-controlled reactions are reversible. The enzymes affect only the
rate of biochemical reactions, not the direction. e.g., Lipase can catalyse splitting of fat into fatty acids and
glycerol as well as synthesis of fatty acids and glycerol into fats.

Do You Know ?
Highest turn over number is of carbonic anhydrase (36 million/min or 600000 per second) and lowest is of
lysozymes (30/min or 0.5 per second). So carbonic anhydrase is fastest enzyme and lysozymes is
slowest enzyme.

4.7 Factors affecting the enzyme activity :


Hydrogen ion concentration (pH) : Some enzyme act best in an acid medium,
other in an alkaline medium, for every enzyme there is an optimum pH where
its action is maximum e.g., 2 for pepsin, 6.8 for salivary amylase, 8.5 for
trypsin. Most enzyme show maximum activity in a pH range of about 6.0 to 7.5
i.e., near neutral pH (endoenzymes).

Temperature : Within certain limits (5-40°C) the rate of an enzyme catalyzed


reaction increases as the temperature increases. The Q10 of most enzymatic
reactions is 2, i.e., every 10°C rise in temperature doubles the rate of reaction.
Most enzymes show maximum activity in a temperature range of 25 to 40°C.
Beyond this temperature, enzymes becomes denatured but The enzymes are
not destroyed by freezing, and regain their lost activity if the temperature is
raised to normal.

Substrate concentration : If there are more enzyme molecules than substrate molecules, a progressive
increase in the substrate molecules increases the velocity of their conversion to products. However,
eventually the rate of reaction reaches the maximum. At this stage the active sites of all the available
enzyme molecules are occupied by the substrate molecules. Therefore, the substrate molecules occupy
the active sites vacated by the products and cannot increase the rate of reaction further.
NEET_Biomolecules-2 - 53
Michaelis constant : Michaelis and Menten (1913) introduced a constant Km (Michaelis constant). It is a
mathematical derivative or constant which indicates the substrate concentration at which the chemical
reaction catalysed by an enzyme attains half its maximum velocity (Vmax). Km indicates affinity of the
1
enzyme for its substrate. Km = V K value differs from substrate to substrate because different en-
2 max m
zymes differ in their affinity towards different substrates. A high Km indicates low affinity while a low Km
shows strong affinity. Protease acts on different proteins. So it’s Km value will differ from protein to protein.

4.8 Enzyme inhibition :


(i) Competitive inhibition :
Substances (inhibitors) which are structuraly similar to the substrates and competes for the active site
of the enzyme are known as competitive inhibitors.
Usually such inhibitors show a close structural resemblance to the substrates to the enzyme they
inhibit. In such a case, inspite of enzyme substrate complex, enzyme inhibitor complex is formed and
enzyme activity is inhibited.

E (Enzyme) + I (Inhibitor) EI (Enzyme - Inhibitor complex EI)

The concentration of EI complex depends on the concentration of free inhibitor. Because EI complex
readily dissociates, the empty active sites are then available for substrate binding.

The effect of a competitive inhibitor on activity is reversed by increasing the concentration of substrate.
In it Vmax remain constant and Km increases.

A classic example of competitive inhibition is succinic acid dehydrogenase which oxidises


succinic acid to fumaric acid. If concentration of malonic acid, is added, the activity of succinic
dehydrogenase decreases rapidly. Hence malonic acid acts as a competitive inhibitor since it
has structural resemblance to succinic acid.

The competitive inhibition can be reversed by increasing the concentration of the substrate.
Competitive inhibitors are used in control of bacterial pathogens.

(ii) Non-competitive inhibition :

These substances (poisons) do not combine with active sites but attach somewhere else and destroy
the activity of enzyme.
NEET_Biomolecules-2 - 54
Both EI and ES complexes are formed.

Inhibitor binding alters the three dimensional configuration of the enzyme and thus blocks the reaction.

Non competitive inhibitor do not competes directly with the substrate for binding to the enzyme. In it
Vmax in lowered and Km is changed.

The non-competitive inhibition can not be reversed by increasing the concentration of the substrate
i.e., irreversible. e.g., cyanide inhibits the mitochondrial enzyme cytochrome oxidase which is essen-
tial for cellular respiration. This kills the animals.
AMP is a non competitive inhibitor of fructose biphosphate phosphatase, the enzyme that catalyzes the
conversion of fructose 1, 6 biphosphate to fructose 6 phosphate.
(a) Feedback inhibition :
In number of cases, accumulation of the final product of the reaction is capable of inhibiting the first step
of reaction. The product P checks the activity of enzyme which converts A into B. It is quite useful
mechanism because it checks the accumulation of products.

The phenomenon in which the end product of a metabolic pathway can regulate its own production by
inhibition of the sort is called feed back inhibition or negative feed back inhibition.
This type of inhibition can be shown in Escherichia coli bacterium which synthesises the amino acid
isoleucine from a substrate threonine by a series of intermediate reactions (i.e., ketobutyrate threo-
nine deaminase, Aceto hydroxy butyrate, keto methyl valerate etc).
When isoleucine accumulates in amounts more than required, it stops its own production by inhibiting
the activity of the enzyme.
Threonine deaminase which catalyzes the first reaction of the series.
This type of metabolic control in which the first enzyme of a series is inhibited by the end product, is
known as end product inhibition.
(b) Allosteric inhibition (Modulation) :
Allosteric literally means ‘another place’. Still other inhibitors join an enzyme at a specific site and
change the form of the active site meant for the substrate.
These inhibitors are known as modifiers or modulators and the sites where they fit in are called allosteric
sites. Modulators are of two types-positive (activators) and negative (inhibitors).
Change of active site form prevent the binding of substrate to the enzyme and stops the reaction. The
process is called allostery or allosteric inhibition,
The enzyme with allosteric sites are called allosteric enzymes. Jacob and Monod have termed this
phenomenon as allosteric transition.
An example of allosteric enzyme inhibition is hexokinase that converts glucose to glucose 6-
phosphate. Glucose 6-phosphate causes allosteric inhibition of hexokinase. This is called feed-
back allosteric inhibition.

NEET_Biomolecules-2 - 55
Primary metabolites : Substances that is required for growth of living organisms

Secondary metabolites : Substances that is not required (waste material) for growth of living organisms

However, many of them are useful to 'human welfare' (e.g., rubber, drugs, spices, scents and pigments).
Some secondary metabolites have ecological importance.

Some Secondary Metabolites


Pigments Carotenoids, Anthocyanins, etc.
Alkaloids Morphine, Codeine, etc.
Terpenoides Monoterpenes, Diterpenes etc.
Essential oils Lemon grass oil, etc.
Toxins Abrin, Ricin
Lectins Concanavalin A
Drugs Vinblastin, curcumin, etc.
Polymeric substances Rubber, gums, cellulose

Most of the vitamins of B complex group act as coenzyme.

Myosin a structural component of muscle. It has ATPase activity also.


Smallest enzyme oxydase and largest enzyme catalase, which are found in peroxysome.
Synthesis of enzymes occur in polysome (aggregation of ribosomes).
Competitive inhibitor increase Michaelis constant (Km) but it has no effect on Vmax.
Regulators of metabolism are enzymes, vitamins and hormones.
RNA polymerase enzyme form RNA from DNA and DNA polymerase is responsible for synthesis of DNA
from DNA
Enzyme that catalyses the conversion of soluble proteins into insoluble ones, process is called enzyme
coagulation.
Albinism is caused by the deficiency of tyrosinase.
Nitrogenase enzyme is inactivated by oxygen.
Some enzyme are active at very high temperature (70–80°C) called extermozyme e.g., Taq polymerase.
In a polypeptide or a protein, amino acids are linked by a peptide bond which is formed when the
carboxyl (-COOH)group of one amino acid reacts with the amino (–NH2) group of the next amino acid
with the elimination of a water moiety (the process is called dehydration).
In a polysaccharide the individual monosaccharides are linked by a glycosidic bond. This bond is also
formed by dehydration. This bond is formed between two carbon atoms of two adjacent monosaccharides.
In a nucleic acid a phosphate moiety links the 3'-carbon of one sugar of one nucleotide to the 5' -carbon
of the sugar of the succeeding nucleotide.
The bond between the phosphate and hydroxyl group of sugar is an ester bond. As there is one such
ester bond on either side, it is called phosphodiester bond.
Nucleic acids exhibit a wide variety of secondary structures.
For example, one of the secondary structures exhibited by DNA is the famous Watson-Crick model.
This model says that DNA exists as a double helix. The two strands of polynucleotides are antiparallel
i.e., run in the opposite direction. The backbone is formed by the sugar-phosphate-sugar chain. The
nitrogen bases are projected more or less perpendicular to this backbone but face inside.

NEET_Biomolecules-2 - 56
A and G of one strand compulsorily base pairs T and C, respectively, on the other strand.
There are two hydrogen bonds between Aand T. There are three hydrogen bonds between G and C.
Each strand appears like a helical staircase.
Each step of ascent is represented by a pair of bases. At each step of ascent, the strand turns 36°. One
full turn of the helical strand would involve ten steps or ten base pairs. Attempt drawing a line diagram.
The pitch would be 34Å. The rise per base pair would be 3.4A. This form of DNA with the above
mentioned salient features is called B-DNA.
RNA is found in the cytoplasm and nucleolus. Inside the cytoplasm it occurs freely as well as in the
ribosomes.
RNA can also be detected from mitochondria, chloroplasts and associated with the eukaryotic chromo-
somes. In some plant viruses RNA acts as hereditary material.

NEET_Biomolecules-2 - 57
Type (I) : Very Short Answer Type Questions : [01 Mark Each]
1. What is the monomer unit of nucleic acid ?
2. Write the name of bases which are found in DNA
3. What is the main reason of acidic nature of DNA
4. Write the name of nitrogenous bases which are found in RNA.
5. What is the main constituent of most of the enzyme?

Type (II) : Short Answer Type Questions : [02 Marks Each]


6. In which glycosidic bond, peptide bond and phosphodiester bonds are found
7. Write the factors affecting the activity of enzyme.
8. Write the name of the components of nucleotides of DNA & RNA.
9. What are the macromolecules ? Give examples.

Type (III) : Long Answer Type Questions: [03 Mark Each]


10. What are the enzyme inhibitors ? explain.
11. On the basis of reaction which are the classes of enzyme?
12. Write three points related to structure of DNA.

Type (IV) : Very Long Answer Type Questions: [05 Mark Each]
13. Write the labelled diagram of watson & crick model of DN A.
14. Explain the different points of catalytic cycle of enzyme action.
15. Write short note an following:-
(1) Co-factor

(2) Metabolites
16. Describe the properties of enzyme.

OBJECTIVE QUESTIONS
Nucleotides and Nucleic acid
1. A ribose (but not deoxyribose) nucleotide is
(1) Cytosine — pentose sugar — phosphate (2) Guanine — pentose sugar — phosphate
(3) Thymine — pentose sugar — phosphate (4) Uracil — pentose sugar — phosphate
2. Which one of the following pairs is not correctly matched
(1) Recombinant DNA DNA formed by the joining of segments of DNA from different sources
(2) Purine Nitrogenous bases Cytosine, thymine and uracil
(3) ATP The principal energy carrying compound in the cell
(4) r-RNA RNA molecules found in ribosomes

NEET_ Biomolecule-2 58
3. DNA differs from RNA
(1) In the nature of sugar alone (2) In the nature of purines alone
(3) In the nature of sugar and pyrimidines (4) None of the above
4. ATP is
(1) Adenosine D-ribose three phosphate (2) Adenosine L-ribose three phosphate
(3) Adenine D-ribose three phosphate (4) Adenine L-ribose three phosphate
5. Thymine is a
(1) Enzyme (2) Vitamin (3) Pyrimidine (4) Purine
6. DNA is concentrated in
(1) Chromatin as DNA protein complex (2) Ribosomes
(3) Golgi bodies (4) Plastids
7. RNA contains
(1) Hexose sugar (2) Deoxyribose sugar (3) Dextrose sugar (4) Ribose sugar
8. In DNA guanine pairs with
(1) Cytosine (2) Thymine (3) Uracil (4) Adenine
9. DNA strands are antiparallel because of the presence of
(1) H-bonds (2) Peptide bonds (3) Disulfide bonds (4) Phosphate-diester bonds
10. Nucleic acids were discovered by
(1) Watson and Crick (2) Khorana (3) Wilkins (4) Miescher
11. DNA is not found in
(1) Chromatin (2) Nucleus (3) Nucleolus (4) Cytoplasm
12. The base pairs of DNA are correctly shown as
(1) A T and C = G (2) A = T and C = G (3) A = T and C G (4) A T and C G
13. Purines are
(1) Single ring compounds (2) Double ring compounds
(3) Straight chain compounds (4) None of the above
14. Which of the following is capable of self replication
(1) An enzyme (2) A carbohydrate molecule
(3) A water molecule (4) A nucleic acid
15. Ultraviolet light absorbed by nucleic acid is
(1) 26 nm (2) 75 nm (3) 260 nm (4) 1500 nm
16. The nucleic acid base having two possible binding sites is
(1) Thymine (2) Cytosine (3) Guanine (4) Adenine
17. The strongest evidence that DNA is genetic material comes from
(1) That chromosomes are made up of DNA (2) Transformation of bacterial cells
(3) That DNA is not present in the cytoplasm (4) That DNA is present in the nucleus
18. A nucleoside differs from a nucleotide in not having
(1) Phosphate (2) Sugar
(3) Phosphate and sugar (4) Nitrogen base

NEET_ Biomolecule-2 59
19. The similarity between DNA and RNA is that both are
(1) Double stranded (2) Having similar sugars
(3) Polymers of nucleotides (4) Having similar pyrimidines
20. Which of the cell organelles are devoid of deoxy ribonucleic acid
(1) Mitochondria and nucleus (2) Chloroplast and mitochondria

(3) Nucleus and chloroplast (4) Lysosome and dictyosome


21. RNA is absent in
(1) Plasmalemma (2) Cytoplasm (3) Chromosomes (4) Ribosomes

ENZYME
22. Who first used the term “enzyme’’
(1) J.B. Sumner (2) Kuhne (3) Thompson (4) Garnier
23. Who coined the term zymase for enzymes in yeast
(1) Kuhne (2) Sumner (3) Louis pasteur (4) Edward Buchner
24. All enzymes contain -
(1) Sugars (2) Proteins (3) Fats (4) Vitamins
25. “Enzymes are proteins’’, it was suggested by
(1) Miller (2) Sumner (3) Pasteur (4) Leeuwenhock
26. Who got the Nobel prize working on enzymes in the year 1978
(1) W. Arber and D. Nathans (2) Nass and Nass
(3) R. Mishra (4) H.G. Khorana
27. Name the scientist who for the first time isolated and purified the enzyme urease in crystalline form from
Jack bean (Canavalia ensiformis)
(1) Kuhne (1826) (2) Hayashi (1826) (3) Kurosawa (1926) (4) Sumner (1926)
28. Which of the following is called “biological middle man’’
(1) Hormone (2) Vitamin (3) Enzyme (4) All the above
29. Who demonstrated that alcoholic fermentation was an enzymatic process
(1) Louis Pasteur (2) Justus Liebeg (3) Edward Buchner (4) James Sumner
30. Enzymes were discovered for the first time in
(1) Yeast (2) Maize (3) Bacteria (4) Algae
31. Who discovered 'co-enzymes’
(1) James Sumner (2) Fritz Lipmann (3) Mayerhoff (4) Edward Buchner
32. Which one of the following statements is true for the enzymes
(1) All enzymes are proteins (2) All proteins are enzymes
(3) All enzymes are not proteins (4) All enzymes are vitamins
33. Enzyme are best defined as
(1) Catalysts (2) Organo–catalysts (3) Protein–catalysts (4) Metallo–catalysts
34. In plants, enzymes are present
(1) Only in flowers (2) Only in leaves
(3) In all the living cells of plant body (4) Only in parenchyma

NEET_ Biomolecule-2 60
35. Biological catalysts are called
(1) Auxins (2) Gibberellins (3) Enzymes (4) All the above
36. Enzymes are the polymers of
(1) 6- carbon (2) Fatty acids (3) Amino acids (4) Inorganic phosphate
37. Which of the following statements is not correct
(1) All enzymes are proteins (2) All enzymes are biocatalysts
(3) All proteins are enzymes (4) All enzymes are thermolabile
38. cAMP mediated 'Cascade model’ of enzyme regulation was proposed by
(1) Fischer (2) Sutherland (3) Sumner (4) Koshland
39. Synthesis of enzymes take place by
(1) Transamination (2) Deamination (3) Translation (4) None of the above
40. Enzymes are absent in
(1) Algae (2) Fungi (3) Bacteria (4) Virus
41. Which one of the following enzyme is not composed of simple proteins
(1) Amylase (2) Pepsin (3) Urease (4) None of the above
42. Enzymes are useful to plants because
(1) They are building block of chlorophyll (2) They are essential for the metabolic processes
(3) They enhance absorption of water and salts (4) They are responsible for paratonic movements
43. Which of the following is not an attribute of enzymes
(1) They are proteinaceous in nature (2) They speed up the rate of biochemical reactions
(3) They are specific in nature (4) They are used up in reactions
44. What is correct about enzymes
(1) They are most active at pH 7.0 (2) They are all amino acids
(3) They are all proteins (4) They are most active at a temperature of 0°C
45. Enzymes are different from inorganic catalysts
(1) Not being used up in reactions (2) Being proteinaceous in nature
(3) Having high diffusion rate (4) Working at high temperature
46. The enzyme used for alcohol formation by fermantation is
(1) Invertase (2) Lipase (3) Amylase (4) Zymase
47. Of the total enzymes present in the cell approximately how many occur in mitochondrion
(1) 10% (2) 30% (3) 50% (4) 70%
48. An average living cell contains about
(1) More than 1000 enzymes (2) More than 2000 enzymes
(3) More than 3000 enzymes (4) More than 5000 enzymes
49. The catalytic efficiency of two different enzymes can be compared by the
(1) Formation of the product (2) The pH of optimum value
(3) The Km value (4) Molecular size of the enzyme
50. Which of the following is not a part of enzyme but it activates the enzyme
(1) K (2) Zn (3) Mg (4) Mn

NEET_ Biomolecule-2 61
51. Huge amount of starch is deposited in potato tubers due to
(1) Chemical condensation of sugars (2) Enzymatic transformations
(3) Synthesis of starch in tubers (4) Absorption of nutrients
52. Which one of the following is an enzyme
(1) Insulin (2) Riboflavin (3) Griseofulvin (4) Lipase
53. An enzyme can be synthesised by chemically bonding together molecules of
(1) Carbohydrates (2) Amino acids (3) Lipases (4) CO2
54. A dialysable non-protein organic substance which combines with apoenzyme to make a functional enzyme
is
(1) Hormone (2) Coenzyme or vitamin(3) Proenzyme (4) Prosthetic group
55. Most enzymes consist of two parts; these are
(1) Enzyme and substrate (2) Enzyme and coenzyme
(3) Apoenzyme and enzyme (4) Apoenzyme and prosthetic group
56. The protein part of enzyme is known as
(1) Holoenzyme (2) Apoenzyme (3) Isoenzyme (4) All of the above
57. Enzyme complex is called
(1) Holoenzyme (2) Apoenzyme (3) Coenzyme (4) Prosthetic group
58. When coenzyme is combined with apoenzyme, it is called
(1) Cofactor (2) Holoenzyme
(3) Substrate enzyme complex (4) Vitamin A
59. Non-protein part of an enzyme is known as
(1) Holoenzyme (2) Apoenzyme (3) Coenzyme (4) All the above
60. The enzyme, which combines with non-protein part to form a functional enzyme known as
(1) Co-enzyme (2) Holoenzyme (3) Apoenzyme (4) Prosthetic group

CLASSIFICATION AND FACTORS AFFECTING ENZYME


61. Term – ase is used for
(1) Classification of enzymes (2) Enzymes with special function
(3) Nomenclature of enzymes (4) All the above
62. Systematic approach of naming enzymes has been recommended by the Commission on Enzymes of the
(1) International Union of Physiology (2) International Union of Biochemistry
(3) International Union of Biotechnology (4) International Union of Genetic Engineering
63. Basically how many types of enzymes have been recognised by International Union of Biochemistry
(1) 4 (2) 5 (3) 6 (4) 8
64. In the modern system of nomenclature which one of the following enzyme occupies 1st position
(1) Oxidoreductase (2) Transferase (3) Hydrolase (4) Ligase
65. The plant proteinases or endopeptidases enzyme is
(1) Urease (2) Papain (3) Pepsin (4) Trypsin
66. Nitrate reductase enzyme is responsible for the formation of
(1) N2 (2) NO2 (3) NO3 (4) Ammonia

NEET_ Biomolecule-2 62
67. The first enzyme that reduces nitrates into nitrites and ammonia in plants is
(1) Nitrate reductase (2) Nitrite reductase
(3) Glutamine synthetase (4) Glutamate dehydrogenase
68. The enzyme responsible for atmospheric nitrogen fixation is
(1) Nitrogenase (2) Hydrogenase (3) Oxygenase (4) Carboxylase
69. At the time of cotton seeds germination, the stored food is digested by
(1) Diastase (2) Maltase (3) Lipase (4) Amylase
70. Substrate of amylase enzyme is
(1) Protein (2) Fat (3) Starch (4) Sucrose
71. Enzyme which hydrolyses starch to maltose is
(1) Lactase (2) Protease (3) Maltase (4) Amylase
72. Which one is not an example for hydrolases
(1) Dehydrogenase (2) Protease (3) Amylase (4) Esterase
73. In the cell digestive enzymes are mostly in
(1) Lysosome (2) Cell wall (3) Ribosome (4) Chromosomes
74. Enzyme concerned with transfer of electrons are
(1) Hydrolase (2) Dehydrogenase (3) Transaminase (4) Desmolase
75. Which one of the following belongs to transferase group
(1) Amylase (2) Transaminase (3) Citrate synthetase (4) Enolase
76. Esterase enzyme belongs to which of the following class
(1) Oxidoreductase (2) Carboxylase (3) Hydrolases (4) Transferases
77. Fumerase enzyme belongs to which class
(1) Oxidase (2) Carboxylase (3) Transferase (4) Lyases
78. Enzyme phosphoglucomutase belongs to
(1) Oxidase (2) Lipase (3) Carboxylase (4) Isomerase
79. Which one belongs to hydrolase group
(1) Amylase (2) Transaminase (3) Citrate synthetase (4) Enolase
80. The enzyme which converts proteins into peptones is
(1) Erypsin (2) Pepsin (3) Trypsin (4) Lipase
81. Histone is a protein mainly contains :-
(1) Methionin & serine (2) Glycine & valine
(3) Cysteine & serine (4) Glysine & arginine
82. Which is odd, among the following:-
(1) Adenosine – Adenylic acid (2) Thymidine – Thymidylic acid
(3) Guanine – Guanylic acid (4) Cytidine – Cytidylic acid
83. Enzyme catalyst differ from inorganic catalyst in many ways, but one major difference is that :-
(1) Enzyme specific for pH while inorganic catalyst are not.
(2) Enzyme are mainly made up of protein but inorganic catalysts are not made up of protein.
(3) Enzymes get damaged at high temperatures but inorganic catalysts work efficiently at hight tempera-
ture an high pressure
(4) All of the above.

NEET_ Biomolecule-2 63
84. Enzyme inhibitor which resemble to the structure of substrate, that is :-
(1) Allosteric inhibitor (2) Competitine inhibitor
(3) Non competitive inhibitor (4) All of the above
85. Enzyme which catalyze tranformation of another gruop, other than hydrogen.
(1) Dehydrogenase (2) Lyases (3) Transferase (4) Isomerase
86. Biosynthetic pathway in which energy is consumed and degradative pathway in which energy is released,
respectively known as :-
(1) Catabolic pathway and anabolic pathway. (2) Anabolic pathway and catobolic pathway
(3) Both (1) & (2) (4) Catabolic pathway
87. Enzymes catalysing the linking together of two compounds, these are :-
(1) Lyases (2) Isomerase (3) Hydrolases (4) Ligases
88. Enzymes which catalyse joining of carbon-oxygen, carbon-sulphar, carbon-nitrogen and phosphorus-oxygen-
(1) Ligases (2) Lyases (3) Isomerase (4) Hydrolases
89. The strand turns at which angle in each step of ascent of DNA?
(1) 360º (2) 3.6º (3) 36º (4) None of these

OBJECTIVE QUESTIONS
oLrqfu"B iz'u ¼OBJECTIVEQUESTIONS½
1. Co-enzyme A, which combines with the acetyl group, is formed in part from (4th NSO II L)
(1) Zinc (2) Iron (3) Vitamin A (4) One of the vitamin B
2. Hydrogen boding plays an important structural and functional role in : (2nd NSEB)
(1) DNA (2) Water (3) proteins (4) all of these
3. Water solubility of the DNA molecule is due to: (4nd NSEB)
(1) Deoxy-sugars (2) N-containing base (3) phosphate groups (4) all of these

4. The chemical structure shown in the figure is: (1st CBO)


(1) a tripphosphopeptiide
(2) a ribosugar
(3) deoxyadenosine triphosphate

(4) the nitrogenous base, adenine


(5) deoxythymidine triphosphate

5. A and B in the given graph are the action spectra of


the two enzymes. The two enzymes are (2nd NSEB)

(1) A : amylase B: trypsin


(2) A: pepsin B: trypsin
(3) A: chymotrypsin B: Renin
(4) A: lactate dhydrogenase B: amylase

NEET_ Biomolecule-2 64
AIIMS CORNER
1. The given graph shows the effect of substrate concentration on the rate of reaction of the enzyme green-
gram-phosphatase (AIIMS - 2005)

What does the graph indicate?


(1) The rate of enzyme reaction is directly proportional to the substrate concentration
(2) Presence of an enzyme inhibitor in the reaction mixture
(3) Formation of an enzyme-substrate complex
(4) at higher substrate concentration the pH increases
2. The figure given below shows three velocity substrate concentration curves for an enzyme reaction, What
do the curves a, b, and c depict respectively ? (AIIMS -2006)

(1) a-normal enzyme reaction, b-competitive inhibition, c-non-competitive inhibition,


(2) a-enzyme with an allosteric modulator added, b-norrnal enzyme activity, c-competitive inhibition
(3) a-enzyme with an allosteric stimulator, b-cornpetitive inhibition added, c-normal enzyme reaction
(4) a-normal enzyme reaction, b-non-competitive inhibitor added, c-allosteric inhibitor added
3. An example of competitive inhibition of an enzyme is the inhibition of (AIIMS - 2007)
(1) succinic dehydrogenase by malonic acid (2) cytochrome oxidase by cyanide
(3) hexokinase by glucose-6-phosphate (4) carbonic anhydrase by carbon dioxide.
4. Match the following (AIIMS - 2007)
(a) tRNA 1. Linking of amino acids
(b) mRNA 2. Transfer of genetic information
(c) rRNA 3. Nucleolar organising region
(d) Peptidyl transferase 4. Transfer of amino acid from cytoplasm to ribosome
Options :
(1) a-4, b-2, c-3, d-1 (2) a-1, b-4, c-3, d-2 (3) a-1, b-2, c-3, d-4 (4) a-1, b-3, c-2, d-4

NEET_ Biomolecule-2 65
5. Enzymes, vitamins and hormones can be classified into a single category of biological chemicals because
of all of these (AIIMS 2008)
(1) enhance oxidative metabolism
(2) are conjugated proteins
(3) are exclusively synthesised in the body of a living organism as at present
(4) help in regulating metabolism.
6. If T = 40%, C = 10% then G =? in a pollen cell (AIIMS 2011)
(1) 40% (2) 10% (3) 91% (4) 20%

In each of the following questions a statement of Assertion (1) is given followed by a corresponding
statement of Reason (R) just below it. Of the statements, mark the correct answer as
(1) If both assertion and resaon are true and reason is the correct explanation of assertion
(2) If both assertion and reason are true but reason is not the correct explanation of assertion
(3) If assertion is true but reason is false
(4) If both assertion and reason are false.
7. Assertion : Enzymes lower the activation energy.
Reason: A substrate molecule can be acted upon by a particular enzyme.

(1) (2) (3) (4)

8. Assertion : The higher the turn-over number the more efficient an enzyme is.
Reason: It is not dependent upon the number of active sites present over an enzyme.

(1) (2) (3) (4)

9. Assertion : Enzyme becomes inactive below minimum temperature.


Reason: The inactivity of the enzymes is due to denaturation.

(1) (2) (3) (4)


10. Assertion : DNA molecules and RNA molecules are found in the nucleus of cell.
Reason: On heating, enzymes do not lose their specific activity. [AIIMS 1994]

(1) (2) (3) (4)


11. Assertion : Enzymes are defined as biological proteins.
Reason: Chemically all enzymes are globular proteins. [AIIMS 1997]
(1) (2) (3) (4)
12. Assertion : Enzymes have active sites and substrates reactive sites, on their surfaces respectively.
Reason: Active and reactive sites push the enzyme and substrate molecules away from each other :
[AIIMS 1999]
(1) (2) (3) (4)
13. Assertion : Competitive inhibitor is also called as substrate analogue. (AIIMS 2008)
Reason : It resembles the enzymes In structure.
(1) (2) (3) (4)
14. Assertion : Allosteric enzymes show feed back inhibition. (AIIMS 2012)
Reason : The inhibitor is competitive.
(1) (2) (3) (4)

NEET_ Biomolecule-2 66
PART- 1

1. RNAdoes not possess (AIMPT-1988)


(1) uracil (2) thymine (3) adenine (4) cytosine
2. In double helix of DNA, the two DNA strands are (AIMPT-1988)
(1) coiled around a common axis (2) coiled around each other
(3) coiled differently (4) coiled over protein sheath
3. Which is not consistent with double helical structure of DNA? (AIMPT-1990)
(1) A = T, C = G (2) Density of DNAdecreases on heating
(3) A + T/C + G is not constant (4) Both (1) and (2)
4. The basic unit of nucleic acid is (AIMPT-1991)
(1) pentose sugar (2) nucleoid (3) nucleoside (4) nucleotide
5. A nucleotide is formed of (AIMPT-1991)
(1) purine, pyrimidine and phosphate (2) purine, sugar and phosphate
(3) nitrogen base, sugar and phosphate (4) pyrimidine, sugar and phosphate
6. DNAis composed of repeating units of (AIMPT-1991)
(1) ribonucleosides (2) deoxyribonucleosides(3) ribonucleotides (4) deoxyribonucleotides
7. In RNA, thymine is replaced by (AIMPT-1991)
(1) adenine (2) guanine (3) cytosine (4) uracil
8. A segment of DNA has 120 adenine and 120 cytosine bases. The total number of nucleotides present in
the segment is (AIMPT-1991)
(1) 120 (2) 240 (3) 60 (4) 480
9. Adenine is (AIMPT-1992)
(1) purine (2) pyrimidine (3) nucleoside (4) nucleotide
10. Amino acids are produced from (AIMPT-1992)
(1) proteins (2) fatty acids (3) essential oils (4) -keto acids
11. Which is distributed more widely in a cell? (AIMPT-1992)
(1) DNA (2) RNA (3) Chloroplasts (4) Spherosomes
12. Which is wrong about nucleic acids? (AIMPT-1993)
(1) DNAis single stranded in some viruses (2) RNA is double stranded occasionally
(3) Length of one helix is 45 Å in B-DNA (4) One turn of Z-DNAhas 12 bases
13. Which one contains four pyrimidine bases ? (AIMPT-1994)
(1) GATCAATGC (2) GCUAGACAA (3) UAGCGGUM (4) TGCCTMCG
14. Two free ribonucleotide units are interlinked with (AIMPT-1995)
(1) peptide bond (2) covalent bond (3) hydrogen bond (4) phosphodiester bond
15. Most diverse macromolecules, found in the cell both physically and chemically are (AIMPT-1996)
(1) proteins (2) carbohydrates (3) nucleic acids (4) lipids

NEET_ Biomolecule-2 67
16. The nitrogenous organic base purine occurring in RNA is (AIMPT-1996)
(1) cytosine (2) thymine (3) guanine (4) uracil
17. Genes are packaged into a bacterial chromosome by (AIMPT-1997)
(1) histones (2) basic proteins (3) acidic proteins (4) actin
18. The RNA that picks up specific amino acids from the amino acid pool in the cytoplasm to ribosome
during protein synthesis is called (AIMPT-1997)
(1) mRNA (2) tRNA (3) rRNA (4) carrier RNA
19. The transfer RNA molecule in 3D appears (AIMPT-2000)
(1) L-shaped (2) E-shaped (3) V-shaped (4) S-shaped
20. Length of one turn of the helix in a B-form DNA is approximately (AIMPT-2000)
(1) 3.4 nm (2) 2 nm (3) 0.34 nm (4) 20 nm

21. One of the similarities between DNA and RNA is that both (AIMPT-2000)
(1) are polymers of nucleotides (2) are capable of replicating
(3) have similar sugars (4) have similar pyrimidine bases
22. ATP is a (AIMPT-2000)
(1) nucleotide (2) nucleosome (3) nucleoside (4) purine
23. Types of RNA polymerase required in nucleus for RNA synthesis (AIMPT-2000)
(1) 1 (2) 2 (3) 3 (4) 4
24. Due to discovery of which of the following in 1980 the evolution was termed as RNA world? (AIMPT-2001)
(1) mRNA, tRNA, rRNA synthesize proteins (2) In some virus RNA is genetic material
(3) RNA have enzymatic property (4) RNA is not found in all cells
25. Sequence of which of the following is used to know the phylogeny? (AIMPT-2002)
(1) mRNA (2) rRNA (3) tRNA (4) DNA

26. If DNApercentage of thymine is 20.What is the percentage of guanine ? (AIMPT-2002)


(1) 20% (2) 40% (3) 30% (4) 60%

27. Which form of RNAhas a structure resembling clover leaf ? (AIMPT-2004)


(1) rRNA (2) hnRNA (3) mRNA. (4) tRNA
28. Nucleotides are building blocks of nucleic acids. Each nucleotide is a composite molecule formed by
(AIMPT-2005)
(1) base-sugar-phosphate (2) base-sugar-OH
(3) (base-sugar-phosphate) (4) sugar-phosphate
29. Antiparallel strands of a DNA molecule means that (AIMPT-2006)
(1) the phosphate groups of two DNA strands, at their ends, share the same position
(2) the phosphate groups at the start of two DNA strands are in opposite position (pole)
(3) one strand turns clockwise
(4) one strands turns anti-clockwise
30. One turn of the helix in a B-form DNA is approximately (AIMPT-2006)
(1) 0.34 nm (2) 3.4 nm (3) 2 nm (4) 20 nm
31. The two polynucleotide chains in DNA are (AIMPT-2007)
(1) parallel (2) discontinuous (3) antiparallel (4) semiconservative

NEET_ Biomolecule-2 68
32. About 98 percent of the mass of every living organism is composed of just six elements including carbon,
hydrogen, nitrogen, oxygen and (AIMPT-2007)
(1) phosphorus and sulphur (2) sulphur and magnesium
(3) magnesium and sodium (4) calcium and phosphorus
33. In the DNA molecule (AIMPT-2008)
(1) the total amount of purine nucleotides and pyrimidine nucleotides is not always equal
(2) there are two strands which run parallel in the 5' 3’ direction
(3) the proportion of adenine in relation to thymine varies with the organism
(4) there are two strands which run antiparallel-one in 5' 3' direction and other in 3' 5'

Enzymes
34. Which of the following is not a part of enzyme but it activates the enzyme? (AIMPT-1989)
(1) K (2) C (3) N (4) Si

35. Enzymes having slightly different molecular structure but performing identical activity are (AIMPT-1991)
(1) homoenzymes (2) isoenzymes (3) apoenzymes (4) coenzymes
36. An enzyme brings about (AIMPT-1993)
(1) decrease in reaction time (2) increase in reaction time
(3) increase in activation energy (4) reduction in activation energy
37. What is common among amylase, rennin and trypsin? (AIMPT-1997)
(1) These are all proteins (2) These are proteolytic enzymes
(3) These are produced in stomach (4) These act at a pH lower than 7
38. Cofactor (coenzyme) is a part of holoenzyme it is (AIMPT-1997)
(1) loosely attached inorganic part
(2) accessory non-protein substance attached firmly
(3) loosely attached organic part
(4) None of the above
39. Enzymes are absent in (AIMPT-2000)
(1) algae (2) fungi (3) cyanobacteria (4) viruses
40. Enzymes enhance the rate of reaction by (AIMPT-2000)
(1) forming a reactant-product complex
(2) changing the equilibrium point of the reaction
(3) combining with the product as soon as it is formed
(4) lowering the activation energy of the reaction
41. Feedback inhibition of an enzymatic reaction is caused by (AIMPT-2000)
(1) end product (2) substrate (3) enzyme (4) rise in temperature
42. Enzyme first used for nitrogen fixation is (AIMPT-2001)
(1) nitrogenase (2) nitroreductase (3) transferase (4) transaminase
43. Hydrolytic enzymes which act at low pH are called as (AIMPT-2002)
(1) proteases (2) -amylases (3) hydrolases (4) peroxidases
44. Which of the following enzymes are used to join bits of DNA? (AIMPT-2002)
(1) Ligase (2) Primase (3) DNA polymerase (4) Endonuclease

NEET_ Biomolecule-2 69
45. Which one of the following hydrolyses internal phosphodiester bonds in a polynucleotide chain?
(AIMPT-2005)
(1) Lipase (2) Protease (3) Endonuclease (4) Exonuclease
46. Which of the following statements regarding enzyme inhibition is correct? (AIMPT-2005)
(1) Competitive inhibition is seen when a substrate competes with an enzyme for binding to an inhibitor
protein
(2) Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the
enzyme
(3) Non-competitive inhibition of an enzyme can be overcome by adding large amount of substrate
(4) Non-competitive inhibitors often bind to the enzyme irreversibly
47. Enzymes, vitamins and hormones can be classified into a single category of biological chemicals,
because all of these (AIMPT-2005)
(1) help in regulating metabolism
(2) are exclusively synthesized in the body of a living organism as at present
(3) are conjugated proteins
(4) enhance oxidative metabolism
48. The catalytic efficiency of two different enzymes can be compared by the (AIMPT-2005)
(1) formation of the product (2) pH optimum value
(3) Km value (4) molecular size of the enzyme
49. Telomerase is an enzyme which is a (AIMPT-2005)
(1) repetitive DNA (2) RNA (3) simple protein (4) ribonucleoprotein
50. An organic substance bound to an enzyme and essential for its activity is called (AIMPT-2006)
(1) holoenzyme (2) apoenzyme (3) isoenzyme (4) coenzyme
51. An enzyme that can stimulate germination of barley seeds is (AIMPT-2006)
(1) a-amylase (2) lipase (3) protease (4) invertase
52. Modern detergents contain enzyme preparation of (AIMPT-2008)
(1) acidophiles (2) alkaliphiles (3) thermoacidophiles (4) thermophiles
53. A competitive inhibitor of succinic dehydrogenase is (AIMPT-2008)
(1) malonate (2) oxaloacetate (3) -ketoglutarate (4) malate
54. The linking of antibiotic resistance gene with the plasmid vector became possible with (AIMPT-2008)
(1) DNA ligase (2) endonucleases (3) DNApolymerase (4) exonucleases

NEET_ Biomolecule-2 70
55. The figure given below shows the conversion of a substrate into product by an enzyme. In which one of the
four option (1-4) the components of reaction labelled as A, B, C and D are identitied correctly.
(AIPMT Mains-2010)

Options :

56. Three of the following statements about enzymes are correct and one is wrong which one is wrong
(1) Most enzymes are proteins but some are lipids
(2) Enzymes require optimum pH for maximal activity
(3) Enzymes are denatured at high temperatures but in certain exceptional organisms they are effective
even at temperatures 80°- 90°C
(4) Enzymes are highly specific (AIPMT Mains-2010)

57. In curve of enzyme catalyzed reaction, the value of velocity (AIPMT Mains- 2010)
of enzyme reaction at point A will be

1
(1) V and velocity may increase by increasing tempreture
2 max

1
(2) V and velocity may increase by increasing substrate
2 max

1
(3) V and velocity may increase by increasing by catalyst
2 max

1
(4) V and velocity remain constant even changing any factor into the medium.
2 max

NEET_ Biomolecule-2 71
58. Which one of the following enzymes carries out the initial step in the digestion of milk in humans ?
(AIPMT Pre-2011)
(1) Pepsin (2) Rennin (3) Lipase (4) Trypsin
59. Which of the following is the best evidence for the 'Lock- and-key model' of enzyme action? (AIPMT- 2011)
(1) all isolated enzymes have been identified as proteins
(2) compounds similar in structure to the substrate inhibit the reaction
(3) enzymes are found in living organisms and speed up certain reactions
(4) enzymes determine the direction of reaction
60. The curve given below shows enzymatic activity with relation to three conditions pH, temperature and
substrate concentration. (AIPMT Pre-2011)

What do the two axises (x and y) represent ?


x - axis y-axis
(1) enzymatic activity pH
(2) temperature enzymatic activity
(3) Substrate concentration, enzymatic activity
(4 enzymatic activity temperature
61. Given below is the diagrammatic representation of one of the categories of small molecular weight organic
compounds in the living tissues. Identify the category shown and the one blank component "X" in it.
[AIPMT Pre. 2012]

Category Component
(1) Cholesterol Guanine
(2) Amino acid NH2
(3) Nucleotide Adenine
(4) Nucleoside Uracil

NEET_ Biomolecule-2 72
62. The length of DNA molecule greatly exceeds the dimensions of the nucleus in eukaryotic cells. How is this
DNA accommodated? (CPMT - 2007)
(1) Supercoiling in nucleosomes (2) DNase digestion
(3) Through elimination of repetitive DNA (4) Deletion of non-essential genes
63. Telomere repetitive DNA sequences control the function of eukaryotic chromosomes because they
(CPMT - 2007)
(1) Are RNA transcription initiator (2) Help chromosome pairing
(3) Prevent chromosome loss (4) Act as replicons
64. The Okazaki fragments in DNA chain growth (CPMT - 2007)
(1) Polymerize in the 3' - to - 5' direction and forms replication fork
(2) Prove semiconservative nature of DNA replication
(3) Polymerize in the 5' - to - 3' direction and explain 3' - to 5' DNA replication
(4) Result in transcription
65. A sequential expression of a set of human genes occurs when a steroid molecule binds to the
(CPMT - 2007)
(1) DNA sequence (2) Messenger RNA (3) Ribosome (4) Transfer RNA
66. Molecular basis of organ differentiation depends on the modulation in transcription by (CPMT - 2007)
(1) Ribosome (2) Transcription factor (3) Anticodon (4) RNA polymerase
67. The two polynucleotide chains in DNA are (CPMT - 2007)
(1) Discontinuous (2) Antiparallel (3) Semiconservative (4) Parallel
68. Nucleolus is the site for synthesis of (BHU PMT - 2007)
(1) t-RNA (2) DNA (3) Ribosome (4) m-RNA
69. Histones are (BHU PMT - 2007)
(1) Acidic proteins (2) Basic proteins (3) Mucoproteins (4) Glycoproteins
70. Which one of the following amino acid was not found to be synthesized in Miller's experiment?
(AFMC - 2008)
(1) Glycine (2) Glutamic acid (3) Aspartic acid (4) Alanine
71. Restriction endonuclease (AFMC - 2008)
(1) Cuts the DNA molecule at specific sites
(2) Cuts the DNA molecule randomly
(3) Restricts the synthesis of DNA inside the nucleus
(4) Synthesizes DNA
72. The number of hydrogen bonds between adenine and thymine in a DNA molecule is (CPMT - 2008)
(1) Two (2) Three (3) Four (4) Eight
73. DNA element with ability to change position is called (CPMT - 2008, BHU mains - 2008, UPCPMT-2009)
(1) Cistron (2) Intron (3) Recon (4) Transposon
74. DNA multiplication is called (CPMT - 2008)
(1) Translation (2) Replication (3) Transduction (4) Transcription

NEET_ Biomolecule-2 73
75. Polymerase chain reaction is most useful in (BHU mains - 2008)
(1) DNA synthesis (2) DNA amplification (3) Protein synthesis (4) Amino acid synthesis
76. DNA can not be (BHU mains - 2008)
(1) A-DNA (2) B-DNA (3) Z-DNA (4) Y-DNA
77. The segment of DNA which acts as the instrumental manual for the synthesis of the protein is
(1) Nucleoside (2) Ribose (3) Nucleotide (4) Gene (CBSE - 2009)
78. Which one of the following is the correct matching of three items and their grouping category?
Item Group (CBSE - 2009)
(1) Cytosine, uracil, thiamine Pyrimidines
(2) Malleus, incus, cochlea Ear ossicles
(3) IIlium, ischium, pubis Coxal bones of pelvic girdle
(4) Actin, myosin rhodopsin Muscle proteins
79. During transcription the DNA site at which RNA polymerase binds is called (UP. CPMT - 2009)
(1) Enhancer (2) Regulator (3) Promoter (4) Receptor
80. Formation of m-RNA from DNA is called (UPCPMT - 2009)
(1) Transduction (2) Transformation (3) Translation (4) Transcription
81. DNA nucleotides are attached by (AFMC - 2009)
(1) Hydrogen bonds (2) Vanderwals bond (3) Covalent bond (4) Electrovalent bond
82. Virus envelope is known as (CBSE - 2010)
(1) Virion (2) Nucleoprotein (3) Core (4) Capsid
83. Which one of the following palindromic base sequences in DNA can be easily cut at about the middle by
some particular restriction enzyme ? (CBSE - 2010)
(1) 5' _____ GATATG _____ 3'
3' _____ CTACTA _____ 5'
(2) 5' _____ GAATTC _____ 3'
3' _____ CTTAAG _____ 5'
(3) 5' _____ CACGTA _____ 3'
3' _____ CTCAGT_____ 5'
(4) 5' _____ CGTTCG _____ 3'
3' _____ ATGGTA _____ 5'
84. DNA or RNA segment tagged with a radioactive molecule is called : (CBSE - 2010)
(1) Probe (2) Clone (3) Plasmid (4) Vector
85. Semiconservative mode of replication of DNA was proved by (UPCPMT - 2010)
(1) Hershey and Chase (2) Mescloson and Stahl (3) Griffith (4) Watson and Crick
86. DNA contains nitrogen bases (AFMC 2010)
(1) AGTC (2) AGCU (3) CTAU (4) GAUT
87. Prokaryotic genetic material contain - [CBSE 1999]
(1) neither DNA nor histones (2) DNA but no histones
(3) Either DNA or histones (4) Both DNA and histones
88. Which sugar is present in nucleic acid- [RPMT 2004]
(1) Pentose (2) Hexose (3) Fructose (4) Glucose

NEET_ Biomolecule-2 74
BOARD LEVEL EXERCISE : HINT & SOLUTIONS

1. The monomer unit of nuclic acid is nucliotide.


2. The name of bases which are found in DNA are purine - adenine, guanine. Pyrimidine - cytosine , thymine.
3. The main reason of acidic nature of DNA is phosphate group (phosphoric acid).
4. The name of nitrogenous bases which are found in RNA are purine - adenine, guanine. Pyrimidine -
cytosine , uracil.
5. The main constituent of most of the enzyme is protein
6. Glycosidic bond - DNA
Peptide bond - Protein
Phosphodiester bond - DNA
7. The factors affecting the activity of enzyme - pH, temperature, substrate concentration.
8. The name of the components of nucleotides of DNA Sugar - Dioxyribose, Nitrogenus base - purine -
adenine, guanine. Pyrimidine - cytosine , thymine and phosphoric acid.
The name of the components of nucleotides of RNA Sugar - Ribose, Nitrogenus base - purine - adenine,
guanine. Pyrimidine - cytosine , uracil and phosphoric acid.
9. Those molecules which are found in the acid insoluble fraction is called macromolecules or
biomacromolecules. Example - Protein, Nucleic acid, Polysaccharide.
10. See pg. no. 54
11. See pg. no. 49
12. See pg. no. 42
13. See pg. no. 43
14. See pg. no. 51
15. (1) See pg. no. 48 (2) See pg. no. 45
16. See pg. no. 52

EXERCISE - 1
1. (4) 2. (2) 3. (3) 4. (3) 5. (3) 6. (1) 7. (4)
8. (1) 9. (4) 10. (4) 11. (3) 12. (3) 13. (2) 14. (4)
15. (1) 16. (4) 17. (2) 18. (1) 19. (3) 20. (4) 21. (1)
22. (2) 23. (4) 24. (2) 25. (2) 26. (1) 27. (4) 28. (3)
29. (3) 30. (1) 31. (2) 32. (1) 33. (3) 34. (3) 35. (3)
36. (3) 37. (3) 38. (2) 39. (3) 40. (4) 41. (4) 42. (2)
43. (4) 44. (3) 45. (2) 46. (4) 47. (4) 48. (2) 49. (3)
50. (1) 51. (2) 52. (4) 53. (2) 54. (4) 55. (4) 56. (2)
57. (1) 58. (2) 59. (3) 60. (2) 61. (3) 62. (2) 63. (3)
64. (1) 65. (2) 66. (2) 67. (1) 68. (1) 69. (4) 70. (3)
71. (4) 72. (1) 73. (1) 74. (2) 75. (2) 76. (3) 77. (4)
78. (4) 79. (1) 80. (2) 81. (4) 82. (3) 83. (3) 84. (2)
85. (3) 86. (2) 87. (4) 88. (1) 89. (3)

EXERCISE - 2
1. (4) 2. (4) 3. (3) 4. (3) 5. (2)

EXERCISE - 3
1. (4) 2. (1) 3. (1) 4. (1) 5. (4) 6. (2) 7. (2)
8. (3) 9. (3) 10. (4) 11. (1) 12. (3) 13. (3) 14. (3)

NEET_ Biomolecule-2 75
EXERCISE - 4
1. (2) 2. (1) 3. (3) 4. (4) 5. (3) 6. (4) 7. (4)
8. (4) 9. (1) 10. (4) 11. (2) 12. (3) 13. (1) 14. (4)
15. (1) 16. (3) 17. (2) 18. (2) 19. (1) 20. (1) 21. (1)
22. (1) 23. (3) 24. (3) 25. (2) 26. (3) 27. (4) 28. (1)
29. (2) 30. (2) 31. (3) 32. (1) 33. (4) 34. (1) 35. (2)
36. (4) 37. (1) 38. (3) 39. (4) 40. (4) 41. (1) 42. (1)
43. (3) 44. (1) 45. (3) 46. (2) 47. (1) 48. (3) 49. (4)
50. (4) 51. (1) 52. (2) 53. (1) 54. (1) 55. (3) 56. (1)
57. (2) 58. (2) 59. (2) 60. (2) 61. (4) 62. (1) 63. (3)
64. (3) 65. (1) 66. (4) 67. (2) 68. (3) 69. (2) 70. (2)
71. (1) 72. (1) 73. (4) 74. (2) 75. (2) 76. (4) 77. (4)
78. (1) 79. (3) 80. (3) 81. (1) 82. (4) 83. (2) 84. (1)
85. (2) 86. (1) 87. (2) 88. (1)

NEET_ Biomolecule-2 76

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