BIOMOLECULS

CLASS XII


Introduction
Biomolecules form the basic structural constituent of a living cell. They are
complex organic molecules composed of non-living atoms and molecules, but
organized in a way which allows a living system to grow, sustain and
reproduce itself. A single cell of the bacterium, Escherichia coli contains
about 6,000 different organic compounds. It is believed that man may
contain about 100,000 different types of molecules although only a few of
them have been characterized.
Organic compounds such as amino acids, nucleotides and monosaccharides,
serve as the monomeric units or building blocks of complex biomolecules -
proteins, nucleic acids (DNA and RNA) and polysaccharides, respectively.
Important complex biomolecules like proteins, carbohydrates and fats,
enzymes, vitamins, lipids, hormones and nucleic acids interact with each
other and carry on the biological process of life. Some of the biomolecules
are 'macro molecules'- organic polymers of high molecular weight. Starch,
proteins, nucleic acids are condensation polymers of simple sugars, amino
acids and nucleotides respectively. Most of the biomolecules are very large
and extremely complex. Their reactions involve complex mechanisms.
Some of these interesting facts reveal about the way biomolecules actually
relate to the cell, the fundamental structural and functional unit of living
organisms. Much of the material present in cells is in the form of
biomolecules. Cells need energy for active transport, to move molecules
between the environment and the cells, across cells or within cells. Cells are
also ever-regenerating continuously, dieing and being formed. The complex
reactions of cells revolve around biomolecules and are classified into two
major categories.
The sequence of chemical reactions by which synthesis of various
biomolecules in the cells are achieved is called anabolism. Another series of
reactions called catabolism, usually occurring by different chemical paths,
liberate energy by breaking down of complex organic molecules into smaller
ones and into carbon dioxide and water. Catabolism provides both the
starting materials for anabolism (that act as a fuel for the body) and the
energy needed for various cellular functions carried on by biomolecules. The
complex biomolecules (proteins, lipids, nucleic acids and polysaccharides)
form supramolecular assemblies e.g. membranes, which in turn organize into
organelles, cells, tissues, organs and finally the whole organism.


This entire cycle of chemical synthesis and degradation is known as
metabolism and comes under the domain of Biochemistry.
The Major Complex Biomolecules of Cells
Biomolecule
Building block
(monomeric unit)
Major functions
Carbohydrates
Polysaccharide
(glycogen)
Monosaccharides
(glucose)
Storage (energy to meet short
term demands)
Proteins Amino acids
Fundamental basis of structure
and function of cell (static and
dynamic functions).
Lipids Fatty acids, glycerol
Storage (energy to meet long-
term demands); structural
components of membranes.
Nucleic acids
Deoxyribonucleic acid
(DNA)
Deoxyribonucleotides
Repository of hereditary
information.
Ribonucleic acid (RNA) Ribonucleotides Protein biosynthesis.

In this chapter, we will restrict our study to some of the fundamental
biomolecules and their structures.



Carbohydrates
Carbohydrates are the most abundant organic molecules in nature. They are
primarily composed of the elements carbon, hydrogen and oxygen and are
produced in plants by photosynthesis - the chlorophyll catalyzed combination of
carbon dioxide and water using the energy from sunlight. The name
carbohydrates derives from the fact that most compounds of this type have the
general formula Cx(H2O)y and have hydrogen and oxygen in the same ratio as
water, which projects them as the 'hydrates of carbon'.
Carbohydrates may be defined as polyhydroxy-aldehydes or ketones or
compounds, which produce these on hydrolysis. Carbohydrates supply energy
and serve as part of structural constituents. The term 'sugar' is applied to
carbohydrates soluble in water and sweet to taste.
Functions of carbohydrates
Carbohydrates participate in a wide range of functions.
Carbohydrates are the ultimate source of most of our food and constitute
the most abundant dietary source of energy (4 Cal/g) for all organisms.
Carbohydrates are precursors for many organic compounds (fats, amino
acids).
Carbohydrates (as glyco-proteins and glyco-lipids) participate in the
structure of cell membrane and cellular functions such as cell growth,
adhesion and fertilization.
Carbohydrates also serve as the storage form of energy (glycogen) to
meet the immediate energy demands of the body.
In plants they form as cellulose. We clothe ourselves with cellulose in the
form of cotton, linen and rayon. We build furniture and houses from cellulose
in the form of wood.
Classification of Carbohydrates
Carbohydrates are also referred to as saccharides. They are broadly classified
into 3 groups-monosaccharides, oligosaccharides and polysaccharides. This
categorization is based on the number of sugar units and their behaviour
towards hydrolysis. Mono and oligosaccharides are sweet to taste, crystalline in
character and soluble in water, hence they are commonly known as sugars.

Monosaccharides
These are the basic units of the carbohydrates and are often referred to as
simple sugars as they are sweet in taste. They cannot be broken into simpler
compounds on hydrolysis.
Oligosaccharides
These carbohydrates liberate two to ten monosaccharide molecules on acid
hydrolysis. They are further classified as disaccharides, trisaccharides,
tetrasaccharides, etc., based on the number of monosaccharide units. For
example, disaccharides such as sucrose and lactose are made up of two
monosaccharide units;

There are also tri and tetra saccharides depending on the actual number of
monosaccharide formed when hydrolyzed. For example, a trisaccharide like
raffinose on hydrolysis gives glucose, fructose and galactose.

OLIGOSACCHARIDES - 2 - 10 monosaccharide units

Dissaccharides - 2 monosaccharide units, e.g., Lactose, Maltose,
Cellobiose, Isomaltose, Trehalose, Sucrose

Trisaccharides - 3 monosaccharide units, e.g., Raffinose,
Mannotriose, Rabinose Rhaminose, Gentianose, Melezitose

Tetrasaccharides - 4 monosaccharide units, e.g., Stachyose,
Scorodose

Pentasaccharides - 5 monosaccharide unit, e.g., Verbascose

Polysaccharides
These are carbohydrate polymers with high molecular weight (up to a million)
and on acidic hydrolysis give a very large number of monosaccharide units.
They have the general formula (C
5
H
10
O
5
)
n
, where 'n' is an integer having a very
high value. They are usually amorphous, tasteless (non-sugars) and are
insoluble forming colloids with water. Examples of polysaccharides are cellulose
and starch. Carbohydrates may also be classified as either reducing sugars or
non-reducing sugars.

Reducing Sugars
All those carbohydrates which contain free aldehyde or ketonic group and
reduce Fehling's solution and Tollen's reagent are known as reducing sugars. All
monosaccharides whether aldose or ketose are reducing sugars. Examples are
maltose, lactose.

Non-reducing Sugars
All the carbohydrates which contain no free aldehyde or keto group and are
those molecules which do not reduce Fehling's and Tollen's reagents are non-
reducing sugars. Examples are sucrose, trehalose.
Monosaccharides
Monosaccharides have the general formula C
n
(H
2
O)
n
, crystalline and soluble in
water. They are divided into different categories, based on the functional group
and the number of carbon atoms.
Aldoses
When the functional group in monosaccharides is an aldehyde

They are known as aldoses e.g., glyceraldehyde, glucose.


Ketoses
When the functional group is a keto group, they are referred to as
ketoses e.g., dihydroxyacetone, fructose.

The simplest monosaccharides are Trioses. Glyceraldehyde (triose) the simplest
monosaccharide with one asymmetric carbon atom (A carbon is said to be
asymmetric when it is attached to four different atoms or groups). This has
been chosen as the carbohydrate to represent the structure of all other
carbohydrates.
Glyceraldehydes (the reference carbohydrate) or 2,3-dihydroxypropanal and
dihydroxy-acetone or 1,3-dihydroxypropanone are two well-known trioses. The
structural formulae for these are as follows:

Based on the number of carbon atoms monosaccharides are classified as trioses
(3C), tetroses (4C), pentoses (5C), hexoses (6C) and heptoses (7C).
Carbon Atoms General terms Aldehyde Ketone
3 Triose Aldotriose Ketotriose
4 Tetrose Aldotetrose Ketotetrose
5 Pentose Aldopentose Ketopentose
6 Hexose Aldohexose Ketohexose
7 Heptose Aldoheptose Ketoheptose




Practically, all the monosaccharides that occur in nature contain five or six
carbon atoms i.e. they are 'pentoses' and 'hexoses' respectively.

Structures of Pentoses
The empirical formula of pentoses is C
5
H
10
O
5
. They are of two types.
Aldopentoses
Ketopentoses
The above classification indicates both the name of the carbonyl group and the
number of carbon atoms in the molecule. For example, 'aldopentoses' are five-
carbon monosaccharides with an aldehyde group in the molecule. Examples: D-
Ribose and D-xylose. Similarly, 'ketopentoses' are five carbon atom
monosaccharide with a keto group in the molecule. Examples: D-Ribulose and
D-xylulose.
Structure of Aldo pentoses
D-Ribose
Ribose is wide spread as a constituent of ribonucleic acid and nucleotides.

D-Xylose
Xylose is a constituent of glycoproteins and gums. It is involved in the function
of glycoproteins.

Structure of Keto pentoses
D-Ribulose
It is produced during metabolism. It is an important metabolite in the hexose
monophosphate shunt.

D-Xylulose
It is an important intermediate in the uronic acid pathway.

Structure of Hexoses
The empirical formula of hexoses is C
6
H
12
O
6
. They are also of two types: aldo
hexoses and keto-hexoses. Again the classification indicates both the name of
the carbonyl group and the number of carbon atoms in this molecule.
Aldohexoses' are six-carbon monosaccharides with an aldehyde group in the
molecule. Similarly, 'ketohexoses' are six- carbon monosaccharides with a keto
group in the molecule. Two of the most important monosaccharides are D-
glucose, an aldohexose, and D-fructose, a ketohexose. They are represented by
the open chain structural formula of glucose proposed by Baeyer.
Structure of Aldohexoses
D-Glucose
It is a constituent of polysaccharides and disaccharides. It is also found in
sweet ripe fruits like grapes (up to 30% glucose) and honey.

D-Galactose
It is a constituent of Lactose.

Structure of Ketohexoses
D-Fructose
It is a constituent of sucrose. It is also found in sweet ripe fruits and honey.
Fructose is twice as sweet as sucrose and, in fact is the sweetest of all the
sugars.



Monosaccharides - C
n
H
2n
O
n
. Polyhydroxy aldehydes and
ketones.

Classification according to the nature of carbonyl group.
Aldoses Presence of aldehyde group (-CHO)
Ketoses Presence of ketone group (-C = O)

Classification according to the length of the carbon chain.
Bioses - C
2
H
4
O
2
. 2 C atoms in chain
Trioses - C
3
H
6
O
3
. 3 C atoms in chain
e.g., Glyceraldehyde, Dihydroxyacetone

Tetroses - C
4
H
8
O
4
. 4 C atoms in chain
e.g., Erythrose, Threose.

Pentoses - C
5
H
10
O
5
. 5 C atoms in chain
e.g., D-ribose, D-deoxyribose, L-Arabinose, D-Xylose, D-
Xylulose, D-Ribulose, D-Lyxose.

Hexoses - C
6
H
12
O
6
. 6 C atoms in chain
e.g., D-Glucose, D-galactose, D-Mannose, D-Fructose.

Heptoses - C
7
H
14
O
7
. 7 C atoms in chain,
e.g., Sedoheputlose.
Derived Monosaccharides
Glycosides: OH on C-1 of sugar molecule replaced by other
radicals e.g. Methyl glucosides and Galactosides.

Sugar phosphates: C-1 or C-6 of glucose reacts with H
3
PO
4
(phosphoric acid), e.g., Glucose-1-phosphate and Glucose-6-
phosphate.

Gluconic acid: C-1 in glucose oxidized to carboxyl group.
Glucuronic acid: C-6 in glucose oxidized to carboxyl group.
Amino sugars (hexosamines): Amino group introduced into
hexoses, e.g., Glucosamine, N-acetyl glucosamine, N-acetyl
galactosamine, N-acetyl muramic acid, Neuraminic acid, Sialic
acid.
Preparation of Glucose
Glucose, an aldohexose, is one of the most important monosaccharides. It has
an empirical as well as molecular formula of C
6
H
12
O
6.
It is the main source of
energy for human body and helps in the movement of muscles. It is also the
structural component of some important higher saccharides such as sucrose,
maltose and lactose. It occurs in nature in free as well as combined form
(glucose is present in sucrose, maltose, lactose, starch, cellulose and glycogen)
and is one of the most frequently occurring compounds. It is present in sweet
fruits and honey; for instance, ripe grapes contain ~ 30% of glucose.

Preparation

From cane sugar: When sucrose is boiled with dil. HCl or H
2
SO
4
in alcoholic
solution, one obtains glucose and fructose in equal quantity.

From Starch: When starch is boiled along with dilute H
2
SO
4
at 393 K under
pressure, it hydrolyzes to give glucose. This method is used for commercial
production of glucose.
Structure of Glucose
Glucose has one aldehyde group, one primary and four secondary hydroxyl
groups. The structure of glucose was decided based on the following reactions:
Acetylation of glucose with acetic anhydride gives a penta acetate. This
corroborates the presence of five hydroxyl groups in glucose.


Glucose reacts with hydroxylamine to give monoxime.

Glucose adds a molecule of hydrogen cyanide to give a cyanohydrin.

The presence of a carbonyl group in glucose is proved by these reactions.
Glucose reduces ammoniacal silver nitrate solution (Tollen's reagent) to
metallic silver and also Fehling's solution to reddish brown cuprous oxide and
itself gets oxidized to gluconic acid. This confirms the presence of an aldehydic
group in glucose.

When glucose as well as gluconic acid are reacted with nitric acid, both oxidize
to give saccharic acid which is a dicarboxylic acid. This indicates the presence
of a primary alcoholic group in glucose.

When glucose undergoes protracted heating with HI, it forms n-hexane. This is
indicative of a linear linkage of all the 6 carbon atoms in glucose.

Phenylhydrazine when boiled in acid medium with D-glucose gives glucose
phenyl hydrazone which is soluble. If excess of phenyl hydrazine is used, a
dihydrazone, known as osazone is obtained.

The first two carbons (C
1
and C
2
) are involved in osazone formation. The sugars
that differ in their configuration on these two carbons give the same type of
osazones, since the difference is masked by binding with phenylhydrazine.
On heating with a concentrated solution of NaOH, glucose first turns yellow,
then brown and finally becomes a resin. However, with dilute NaOH, glucose
undergoes a reversible isomerisation and is converted into a mixture of D-
glucose, D-maltose and D-fructose. This reaction is known as Lobry de Bruyn-
van Ekenstein rearrangement. Same results are obtained if maltose or fructose
is treated with alkali. It is probably on account of this isomerisation that
fructose reduces Fehling's and Tollen's reagent in alkaline medium although it
does not contain a -CHO group.

When treated with concentrated sulphuric acid glucose undergoes dehydration
with an elimination of 3 water molecules. Thus hexoses give hydroxymethyl
furfural and pentoses give furfural on dehydration. These furfurals can
condense with phenolic compounds ( -naphthol) to form coloured products.
This is the chemical basis of the popular Molisch test.

Also D-glucose exists in two stereo isomeric forms. These two forms of glucose
differ in crystalline shapes, melting points and optical rotations. This behaviour
could not be explained by the open chain structure for glucose. These two
isomeric forms are due to the presence of anomeric carbons.
Anomeric Carbon
The glucose molecule has four asymmetric (chiral) carbon atoms in the
molecule (the terminal carbon atoms do not hold four different groups and are
not asymmetric. Therefore, glucose will have 2
4
(2
n
where n = number of chiral
carbons) or sixteen optical isomers. A pair of stereoisomers that differ in
configurations around C-1 are called anomers. They differ from each other in
the configuration only around C
1
known as anomeric carbon. In case of
anomer of glucose, the -OH group held by anomeric carbon is on the opposite
side of the group -CH
5
OH of glucose. The reverse is true for -anomer.
The formation of the furfural derivative a ringed compound led to the fact
glucose is involved in some ring formation. It was thought that one of the -OH
groups bonds to the -CHO group to form a hemiacetal structure which is cyclic
in nature. This explains the absence of -CHO group and also existence of
glucose in two forms. The structures of and anomers of carbon are shown
below.

The cyclic forms of D-glucose are known as anomers. However, when
either form is dissolved in water and allowed to stand, the specific rotation of
the solution changes slowly and reaches a constant value at +52.5
o
. This
causes it to change into the other form yielding an equilibrium mixture along
with an extremely low concentration of the open chain form. This equilibrium is
reached faster if a trace of acid or base catalyst is present. The spontaneous
change in specific rotation of an optically active compound is called
mutarotation.

Change
The seemingly insignificant difference in the position of the hydroxyl group on
the ring in and - glucose is of great biochemical importance. Thus, a polymer of
( -glucose known as starch, is easily digested by human beings, whereas the
polymer of -glucose, known as cellulose, is indigestible.
Cyclic Structure of Glucose
The open chain structure of glucose proposed by Baeyer explained most of its
properties. However, it could not explain the following:
Despite having an aldehydic group, glucose does not give Schiff's test and it
does not react with sodium bi-sulphite and ammonia.
The penta acetate of glucose does not react with hydroxylamine indicating
absence of -CHO group.
Mutarotation i.e., the change in the specific optical rotation representing the
inter conversion of forms of D-glucose to an equilibrium mixture.

Monosaccharides do not undergo certain characteristic reactions of aldehydes
and ketones. This is explained on the basis of cyclic structures of
monosaccharides.
Experimental evidences has shown that D-glucose exist mainly in acyclic form
in which two carbon atoms are linked by an oxygen atom. The ring formation
results in two stereoisomers which differ in the orientation of the new hydroxyl
group at the carbonyl carbon atom in the open chain projection. As explained
above such pairs of structures are called anomers. Thus glucose forms a six-
membered ring of five carbon atoms and one oxygen atom (-OH at C-5 is
involved in ring formation) in two forms, known as -glucose and -glucose. The
six membered cyclic structure of glucose is called pyranose structure ( and )
in analogy with pyran, a six membered ring with one oxygen and five carbon
atoms in the ring. These two forms are not mirror
../content/CB12C1/content/topic/ch734/images of each, hence are not
enantiomers. Thus the actual structures of carbohydrates are cyclic and not
open chain.



The six membered cyclic structure of glucose was established by R.D Haworth.
The lower thickened edge of the ring in Haworth structure is nearest to the
observer. The Haworth method of showing the structure is more accurate than
the Fisher formulations. The Haworth projection formulae are the present style
of representing the structures of carbohydrates. The 6 - membered ring is
regarded as an almost regular hexagon with the constituent atoms lying in one
plane. In order to draw Haworth projection formula the hexagon is drawn with
its oxygen atom at the upper right hand corner. All the groups (on C
1
, C
2
, C
3

and C
4
) which are present on the right hand side in the Fisher projection
formulae are placed below the plane of the ring and all those groups on the left
hand side are placed above the plane of the ring. The terminal -CH
2
OH group is
always placed above the plane of the hexagon ring in a D-series.
Structure of Fructose
Fructose is the most important ketose and is isomeric with glucose. Fructose
occurs naturally both in the combined state and free State. In the free state, it
is present along with honey and most sweet fruits and thus the name fruit
sugar. In its combined state fructose is present in sucrose (cane sugar) and
insulin. It is the sweetest monosaccharide. Fructose also has the molecular
formula of glucose - C
6
H
12
O
6
but the fructose molecule has three asymmetric
carbon atoms in the molecule. The formula given here shows D-fructose.

Also eight stereoisomers (four D-, L- pairs) of this formula are known. It is also
named laevulose which signifies that the naturally occurring compound is
laevorotatory. An isomer of fructose represented below has D-configuration and
is laevorotatory.

D-fructose also exists mainly in cyclic form in sucrose as a furanose (5 -
membered ring containing 4 carbon atoms and one oxygen) in which two
carbon atoms are linked by an oxygen atom. The ring formation results in two
stereoisomers, which differ in the orientation of the new hydroxyl group (-OH)
at the carbonyl carbon atom (at C
5
) in the open chain projection.
The cyclic structures of two anomers of fructose are represented by Haworth
structures as given.

It may be noted that fructose can also exists in the pyranose form (6 -
membered ring containing 5 carbon atoms and one oxygen) in free solution.
Glucose Fructose
Points of resemblance
Forms a penta-acetyl
derivative on treatment with
acetic anhydride.
It also forms a penta-acetyl
derivative.
Forms methyl glucose on
treatment with methyl
alcohol and HCl
Forms a similar product called
methyl fructoside on treatment
with methyl alcohol and HCl.
Forms cynohydrin on
treatment with HCN.
Also forms cynohydrin.
Forms oxime with
hydroxylamine NH
2
OH.
Also forms oxime.
Forms glucosazone on
heating with excess of
phenylhydrazine.
Forms exactly similar glucosazone.
On fermentation with yeast
gives ethyl alcohol and CO
2
.
Also forms ethyl alcohol and CO
2

by fermentation in the presence of
yeast.
Reduces Felhing's solution
and ammonical AgNO
3
Also Reduces Felhing's solution and
ammonical AgNO
3
solution.
solution.
Gives n-hexane and 2-
iodohexane on reduction with
HI
Also gives n-hexane and 2-
iodohexane on reduction with HI.
Points of difference
Glucose is dextro-rotatory Fructose is Laevo-rotatory.
Gives sorbitol on reduction
with sodium amalgam and
water.
Gives a mixture of sorbitol and
mannitol.
On oxidation with Br
2
water
gives gluconic acid, which
has the same number of
carbon atoms as glucose.
Not oxidized by mild oxidizing
agents like Br
2
water. On oxidation
with strong oxidizing agents like
conc. HNO
3
it gives acids with
lesser number of carbons than
fructose.
Reacts with lime to give
water-soluble calcium
glucosate.
Forms calcium fructosate, which is
insoluble in water.
Forms a brown resinous mass
with warm NaOH solution.
Does not form a resin with NaOH
solution.

Disaccharides
Among the oligosaccharides, disaccharides are the most common. As is evident
from the namea disaccharide molecule is made up of two monosaccharide
molecules, either the same or different, which have united with the elimination
of one molecule of water. This reaction occurs when one molecule of the
monosaccharide acts as the hemiacetal while the other acts as the alcohol. This
new linkage in the resulting disaccharide molecule is termed as the glycosidic
linkage. Thus, the molecular formula of disaccharides is C
12
H
22
O
11
.

The most common disaccharides are sucrose (cane sugar) made up of glucose
+ fructose, maltose (malt sugar) made up of glucose + glucose, and lactose
(milk sugar) made up of glucose + galactose. Only the above three
disaccharides are known to occur in nature in an uncombined form.

Sucrose (C
12
H
22
O
11
)
Sucrose (cane sugar) is the sugar of commerce, we ordinarily use in foods.
Sucrose or, ordinary table sugar. It is a colourless, crystalline and sweet
substance soluble in water. Sucrose is the sweetest and most abundant among
all the naturally occurring sugars and is extracted from cane sugar (16-20%),
sugar beet (10-15%). It also occurs in nature in pineapple (10-12%), honey,
mango, apricot, and banana.
Sucrose is made up of -D-glucose and -D-fructose. This sugar on acidic
hydrolysis yields one unit of glucose and one unit of fructose, after elimination
of the water molecule. It is held together by a glycosidic bond
between C
1
of -glucose and C
2
of -fructose. The reducing groups of glucose
and fructose are involved in glycosidic bond, so it is a non-reducing sugar and it
cannot form osazones.

Inversion of Cane Sugar
Sucrose, as such is dextrorotatory (+66.5) but when hydrolyzed, it becomes
laevorotatory (-28.2).

The process of change in optical rotation from dextrorotatory (+) to
laevorotatory (-) is referred to as inversion.

Sucrose solution is fermented by yeast when the enzyme invertase hydrolyses
sucrose to glucose and fructose.
Even though the hydrolysis of cane sugar by dilute acids or enzyme invertase,
gives equimolar mixture of D(+) glucose and D(-) fructose, the mixture is
laevorotatory since the laevorotation of fructose (-92.5
o
) is more than
dextrorotation of glucose (+52.5).

Maltose (C
12
H
22
O
11
)
Maltose is obtained by partial hydrolysis of starch by diastase, an enzyme
present in malt (sprouted barley seeds).

In humans, maltose or malt sugar (C
12
H
22
O
11
), as such, is not found in free
form in the body. It is produced during the course of digestion of starch by the
enzyme amylase (pancreatic). Maltose is made up of two -D-glucose (in
pyranose form) units. C
1
of one -glucose units is connected to C
4
of the other
held together by (1 4) glycosidic bond. As there is a free aldehyde group at
C
1
position of the second glucose molecule, maltose is known as reducing
sugar. Maltose forms osazones; it can be hydrolyzed by dilute acid or the
enzyme maltase to liberate two molecules of -D-glucose.

Lactose (C
12
H
22
O
11
)
Lactose is made up of -D-galactose and -D-glucose held together by (1
4) glycosidic bond. As the aldehyde group at C
1
position of glucose is free,
hence lactose exhibits reducing properties and forms osazones.

Lactose known as milk sugar is most important carbohydrate present in milk. It
is an important nutrition for young mammals. Lactase is the enzyme that
hydrolyses lactose. It gets hydrolyzed by emulsin an enzyme which specifically
hydrolyses -glycoside linkages.
Polysaccharides
Polysaccharides are linear as well as branched polymers. The occurrence of
branches in polysaccharides is due to the glycosidic linkages formed at any one
of the hydroxyl groups of a monosaccharide. They are divided into two types:
Homopolysaccharides and Heteropolysaccharides.
Homopolysaccharides
They possess only a single type of monosaccharide units. Starch, cellulose
glycogen, insulin and chitin are homopolysaccharide. They are named based on
the nature of the monosaccharide unit. Thus, glucans are polymers of glucose
whereas fructosans are polymers of fructose.
Heteropolysaccharides
They possess two or more types of monosaccharide units. Heparin and
chondroitin sulphate are examples of heteropolysaccharides. They are also
called as heteroglycans. Heteropolysaccharides on hydrolysis yield a mixture of
a few monosaccharides or their derivatives.
Mucopolysaccharides are the heteroglycans made of repeating units of sugar
derivatives like amino sugars and uronic acids. These are known as
glycosamino glycans (GAG). Important mucopolysaccharides are hyaluronic
acid, chondroitin sulphate and heparin.
Polysaccharides are primarily concerned with two important functions
structural, and storage of energy. In the presence of enzymes or acids, they
change to monosaccharides on complete hydrolysis.
Some examples of polysaccharides are starch, cellulose, glycogen and dextrins.
However the two most widely distributed and important polysaccharides in
nature are starch and cellulose. Starch is an important nutrient for human
beings, and is hydrolyzed in the body by enzymes. Cellulose is the main
structural constituent of plants. Unlike starch, cellulose is not hydrolyzed by the
enzymes in human beings and is, therefore, not digested by them. Grazing
animals, however, do contain the enzymes to hydrolyze cellulose. Both starch
and cellulose are made up of repeating glucose units in different arrangements.
About 200-1000 glucose molecules are linked together to form a starch
molecule; a cellulose molecule is made up of about 3500 glucose units.
Starch
Starch is a homopolymer composed of D-glucose units held by -glycosidic
bonds. It is known as glucosan or glucan. Starch is the carbohydrate reserve of
plants, which is the most important dietary source for higher animals, including
man. High content of starch is found in seeds (cereals), roots, tubers,
vegetables etc. The main sources are wheat, maize, rice, potatoes, barley and
sorghum.
Starch is a white amorphous powder, insoluble in cold water. It solution in
water gives a blue colour with iodine solution. The blue colour disappears on
heating and reappears on cooling. On hydrolysis with dilute acids or enzyme,
starch breaks down into molecules of variable complexity and finally D-Glucose.

Starch does not reduce Fehling's solution or Tollen's reagent and does not form
an osazone indicating that all the hemiacetal hydroxyl group of glucose units
(C
1
) are linked with glycosidic linkages.
Starch consists of two-polysaccharide components water soluble amylose (15-
20%) and a water insoluble amylopectin (80-85%).
Amylose is water soluble, long unbranched (linear) chain with 200-1000 D-
glucose units. These units are joined together by glycosidic linkage
involving C
1
of one glucose unit and C
4
of the other glucose unit. Its molecular
weight can range from 10,000 to 500,000. Amylose gives blue colour with
iodine.

Amylopectin
On the other hand, is water insoluble and a branched chain with
glycosidic bonds at the branching points and linkages everywhere else
on the linear chain. Amylopectin molecule containing a few thousand glucose
units looks like a branched tree (20-30 glucose units per branch). Amylopectin
does not give blue colour with iodine.

Amylase (present in saliva), is the enzyme that hydrolyses starch. It acts
specifically on linkages. The end product of hydrolysis of starch is
glucose which is an essential nutrient.

Cellulose
It is the chief constituent of the cell walls of plants. Wood contains 45-50%
cellulose, while cotton contains 90-95% cellulose. It is a colourless amorphous
solid which decomposes on heating. Cellulose is largely linear and its individual
strands align with each other through multiple hydrogen bonds. This lends
rigidity to its structure. It is thus used effectively as a cell wall material.
Cellulose does not reduce Tollen's reagent or Fehling's solution. It does not
from osazone and is not fermented by yeast. It is not hydrolyzed so easily as
starch but on heating with dilute H
2
SO
4
under pressure yields only D-glucose.
Cellulose is a linear chain composed of -D-glucose units linked by
glycosidic bonds. Cellulose on hydrolysis yields a disaccharide cellobcose and
then produces -D-glucose. Due to the lack of an enzyme that can cleave -
glycosidic bonds, all mammals including man cannot digest cellulose. Large
population of cellulolytic bacteria present in the stomach of ruminant mammals
like cattle, sheep etc., breaks down the cellulose with the help of enzyme
cellulose. It is then digested and converted into glucose.

Glycogen
Glycogen is the carbohydrate reserve in animals, hence often referred to as
animal starch. It is present in high concentration in liver, followed by muscle,
brain etc. Glycogen is also found in plants that do not possess chlorophyll e.g.
yeast, fungi.
The structure of glycogen is similar to that of amylopectin with the two
molecules and their metabolism being virtually identical. The only difference is
that glycogen has more number of branches. Glucose is the repeating unit in
glycogen joined together by (1 4) glycosidic bonds, and (1 6)
glycosidic bonds at branching points.
The supply of glycogen by liver is important in the regulation of blood glucose
levels. After a meal the liver cells take up the excess glucose from the blood
and convert it to glycogen for storage thereby lowering the blood glucose
concentration. Between meals when the blood glucose levels fall the liver cells
break glycogen down to glucose. The glucose is released into the bloodstream,
thereby increasing blood glucose levels.

POLYSACCHARIDES (GLYCANS) - 10 or more monosaccharide
units
Homopolysaccharides (homolycans) - one type of
monosaccharide
Glucans (of glucose monomers) e.g., Starch, Glycogen,
Cellulose, Chitin
Galactans (of galactose monomers) e.g., Agar Pectin
Mannans (of mannose monomers) e.g., Yeast mannans
Xylans (of xylan monomers) e.g., Hemicellulose xylan
Fructans (of fructose monomers) e.g., Inulin.
Heteropolysaccharides (heteroglycans) - two type of
monosaccharide
Neutral sugars - e.g., Hemicelluloses, some Gums,
Mucilagtes, Pectic substances
Mucopolysaccharides - Amino sugars + uronic acid and some
of their derivatives, e.g.,
Hyaluronic acid, Chondroitin sulphates, Heparin. Glycoproteins
- e.g. Plasma proteins,
Blood group substances Mucoproteins

Importance of Carbohydrates
Carbohydrates participate in a wide range of functions:
Carbohydrates are most abundant dietary source of energy (4 Cal/g) for
all organisms. About 60% of the total energy requirement of man is provided
by the breakdown of carbohydrates.
Carbohydrates such as glucose, fructose, starch, glycogen, etc., provide
energy for functioning of living organisms.
They supply energy and also serve as the storage form of energy
(glycogen) to meet the immediate energy demands of the body.
They (as glycoproteins and glyco-lipids) participate in the structure of
cell membrane and cellular functions such as cell growth, adhesion and
fertilization.
They are precursors for many organic compounds (fats, amino acids).
Polysaccharides like cellulose act as chief structural material for cell walls
in plants.
Carbohydrates are utilized as raw materials for several industries e.g.,
paper, plastics, textiles etc.



Proteins
Proteins are the high molecular mass complex biopolymers of amino acids and
organic compounds. They are the most abundant organic molecules of the living
system and form the fundamental basis of structure and function of life. The name
protein is derived from the Greek word proteios meaning 'of prime importance'.
Proteins are present in all living cells of animals and plants and are nitrogen rich
substances having high molecular weight. They occur in every part of the cell and
constituent about 50% of cellular dry weight. Proteins are a major energy source for
growth and maintenance of life. As enzymes, they catalyze biochemical reactions, as
hormones they regulate metabolic processes and as antibodies they protect the body
against toxic substances.
Proteins are the polymers of -amino acids. They are composed of 20 amino acids,
which are repeatedly found in the structure of proteins. Proteins are formed by the
condensation polymerization of more than 100 molecules of amino acids through the
formation of peptide bonds. These amino acids are liberated back when proteins are
hydrolyzed.

All proteins contain the elements carbon, hydrogen, oxygen, nitrogen and sulphur
some of these may also contain phosphorus, iodine, and traces of metals like iron,
copper, zinc and manganese.
Amino Acids
Amino acids are organic compounds that are the building blocks of proteins.
As many as 300 amino acids occur in nature. Among these only 20 are known as
standard amino acids that commonly occur in proteins. This is because of the
universal nature of the genetic code available for the incorporation of only 20 amino
acids when the proteins are synthesized in the cells.
General Structure and Properties
Amino acids contain two functional groups, the amino group and carboxyl group, in
their molecules. The amino group (-NH
2
) is basic and the carboxyl group (-COOH) is
acidic in nature. They are represented by the general formula:

Amino acids are classified as etc., depending upon the position of the
amino group with respect to the carboxyl group. Acids having -NH
2
group attached to
the carbon adjacent to the carboxylic group are termed as -amino acids. Nearly all
the naturally occurring amino acids are -amino acids.

Nomenclature of Amino Acids
Although amino acids can be named according to IUPAC system, they are generally
known by their common names. For example, aminoethanoic acid, NH
2
CH
2
COOH is
better known as glycine rather then -amino acetic acid or 2-amino ethanoic acid.
For the sake of simplicity, each amino acid has been assigned an abbreviation, which
generally consists of the first three letters of the common name. For example,
glycine is abbreviated as Gly. Similarly, alanine CH
3
CH(NH
2
)COOH is abbreviated as
Ala. These trivial names usually reflect the property of that compound or its source.
Example: Glycine is so named since it has sweet taste (in Greek glykos means
sweet).
Structures of some commonly occurring amino acids along with their 3-letter and 1-
letter symbols are given in the following table.
Name of the
amino acids
Characteristic feature of
side chain, R
Three
letter
symbol
One
letter
code
Glycine H Gly G
Alanine -CH
3
Ala A
Valine* (H
3
C)
2
CH- Val V
Leucine* (H
3
C)
2
CH-CH
2
- Leu L
Isoleucine*

Ile I
Arginine*

Arg R
Lysine*

Lys K
Glutamic acid

Glu E
Aspartic acid

Asp D
Glutamine

Gln g
Asparagine

Asn N
Threonine*

Thr T
Serine

Ser S
Cysteine

Cys C
Methionine*

Met M
Phenylalanine*

Phe F
Tyrosine

Tyr Y
Tryptophan*

Trp W
Histidine*

His H
Praline

Pro P

* essential amino acid, a= entire structure
Classification of Amino Acids
There are different ways of classifying the amino acids. One comprehensive
classification of amino acids is based on the structure of the side chains with each
amino acid assigned a 3 letter or 1 letter symbol, as shown in the table above. Other
methods of classification are on the basis of affinity of the side chains for water and
chemical nature (polarity), nutritional requirement, metabolic fate etc.
The twenty amino acids are required for the synthesis of variety of proteins, besides
other biological functions. However, all these 20 amino acids are not needed to carry
on these functions. Based on the nutritional requirements amino acids are grouped
into two classes-essential and non-essential.
Essential Amino Acids
Amino acids which cannot be synthesized by the body and therefore, need to be
supplied through the diet are called essential amino acids. These essential amino
acids are arginine, valine, histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine and tryptophan. Arginine and histidine are called semi-
essential amino acids as they can be partly synthesized in the human body. Lack of
essential amino acids in diet can cause diseases like kwashioker.
Non-essential Amino Acids
The amino acids that can be synthesized by the body to meet the biological needs
called non essential amino acids. About 10 out of 20 amino acids need not be
consumed in the diet; they are: glycine, alanine, serine, cysteine, aspartic acid,
glutamic acid, aspargine, glutamine, tyrosine and proline.
Based on polarity amino acids are classified into four groups.

Non-polar Amino Acids
These amino acids have equal number of amino and carboxyl groups and are neutral.
They are hydrophobic and have no charge on the 'R' group. The amino acids in this
group are alanine, valine, leucine, isoleucine, phenyl alanine, glycine, tryptophan,
methionine and proline.



Polar Amino Acids with no Charge
These amino acids do not have any charge on the 'R' group but are polar due to
reactive functional groups like -OH, -CO-, -SH etc., in them. These amino acids
participate in hydrogen bonding of protein structure. The amino acids in this group
are - serine, threonine, tyrosine, cysteine, glutamine and aspargine.

Polar Amino Acids with Positive Charge
Polar amino acids with positive charge have more amino groups as compared to
carboxyl groups making it basic. The amino acids, which have positive charge on the
'R' group, are placed in this category. They are lysine, arginine and histidine.



Polar Amino Acids with Negative Charge
Polar amino acids with negative charge have more carboxyl groups than amino
groups making them acidic. The amino acids, which have negative charge on the 'R'
group, are placed in this category. They are called as dicarboxylic mono-amino acids.
They are aspartic acid and glutamic acid.


Physical Properties of -Amino Acids
Amino acids are colourless, crystalline solids. They are water-soluble high melting
solids and behave like salts. The -carbon atom has 'R' which is a side chain. This
side chain is different for different amino acids.
Since amino acids contain both a basic group (-NH
2
) and an acidic group (-COOH)
they are amphoteric compounds. They are frequently represented by the structure:

According to this structure, the acidic properties should be due to the group
and basic properties due to - NH
2
group. However, modern researches have shown
that this is incorrect. The acidic properties are due to - NH
2
group and basic
properties are due to the . This is because the proton from the carboxylic
group shifts to the amino group to produce dipolar ion. Such dipolar ion which is
neutral but has both positive and negative charges is called the inner salt or the
zwitter ion.

(Zwitter ion or dipolar structure of amino acid)

In aqueous solution, in the zwitter ionic form, amino acids show amphoteric
behaviour as they react both with acids and bases. In acidic solution, the carboxylate
function (-COO
-
) accepts a proton and gets converted to carboxyl substituent (-
COOH) while in basic solution the ammonium substituent ( H
3
) changes to amino
group (-NH
2
) by losing a proton.


In acidic solution, an amino acid exists as a positive ion and migrates towards the
cathode in an electric field, while in alkaline solution it exists as a negative ion and
migrates towards anode. At a certain hydrogen ion concentration (pH), the dipolar
ion exists as a neutral ion and does not migrate to either electrode. This pH is known
as the isoelectric point of the amino acid.
Iso-electric Point
Isoelectric point of the amino acid is defined as the point at which a molecule exists
as zwitter ion with no net charge. Thus, at this point the molecule is electrically
neutral; it has minimum solubility, maximum precipitability and least buffer capacity.
All amino acids do not have the same isoelectric point. The acidic amino acids and
basic amino acids strongly influence the iso-electric point (PI). The PI value of
protein is determined by the nature of ionisable groups of amino acids. By taking
average pk
a
values of ionisable groups, PI value can be calculated.
The minimum solubility of amino acids in water at the isoelectric point is utilized in
the separation of different amino acids obtained on hydrolysis of proteins. For
example, Leucine has 2 ionizable groups and its iso-electric pH is 6.0 (zwitter ion).
Leucine exists as cation at pH below 6.0 and as anion at pH above 6.0.
If a -carbon atom has four different groups attached to it. Then it is asymmetric
and it exhibits optical isomerism. Except glycine all amino acids exhibit optical
activity. Therefore two stereo isomers are formed and they are mirror
../content/CB12C1/content/topic/ch734/images of each other. They appear as shown
below.

In the 'D' form amino group (NH
2
) is written on the right side and in the 'L' form on
the left side. 'D' and 'L' refer to the configuration of the amino acid molecule about
the asymmetric carbon atom. Most naturally occurring amino acid have L-
configuration.
Structure of Proteins
Proteins are the polymers of -amino acids and they are connected to each other by
peptide bond or peptide linkage. Sometimes the term peptide is employed when the
chain consists of 2 - 10 amino acid residues. Chains containing 10 - 100 amino acid
residues are called polypeptides, and compounds having more than 100 amino acid
residues are called proteins.
Peptide Bond Formation
When two amino acids combine with each other, the amino group of one amino acid
combines with carboxyl group of other amino acid. This leads to peptide bond
formation. The combination of the amino group of one molecule with the carboxyl
group of the other results in the elimination of a water molecule and forms an amide
(-CO-NH-) bond.

The bond formed above is a peptide bond. The dipeptide contains two amino acids
and one peptide bond. The peptide bond can be formed in two different ways. For
example, Glycylalanine (Gly-Ala) has the following structure.

The same two amino acids may also form Ala-Gly where the amino group of glycine
may react with the carboxyl group of alanine. Both those dipeptides have 3 free
functional groups which further react with relevant groups of other amino acids
forming tri, tetra, penta peptides and so on.
Both -CO and -NH groups of peptide bonds are polar. They are involved in hydrogen
bond formation. Peptide bonds are strong, rigid and planar. They have partial double
bond character. They serve as cementing material between individual amino acids.
Peptide chains are written with free amino end at left and free carboxyl end at right.
The polypeptide chain is shown below.

The distance between two adjacent -carbon atoms is 0.36 nm.
Poly Peptides
Molecules containing more than 10 amino acids are called poly peptides. Poly
peptides are formed by the linear sequencing of amino acids. Some proteins are
composed of two or more poly peptide chains. Relatively shorter peptides are known
as oligopeptides whereas longer polymers are called polypeptides. Polypeptides
containing more than 100 amino acids having molecular mass higher then 10,000
are generally called as proteins. However the distinction between a polypeptide and a
protein is not sharp.
As a matter of convention, the structure of peptides is written in a way that the
amino acid with the free amino (-NH
2
) group known as N-terminal residue is written
on the left hand side of the polypeptide chain and the amino acid with the free
carboxyl group (C terminal residue) is written on the right hand side of the chain.
Thus a tripeptide, alanylglycylphenylalanine is represented as follows:

The name of any polypeptide is written starting from the N-terminal residue. The
suffix ine in the name of the amino acid is replaced by '-yl' (as glycine to glycl,
alanine to alanyl etc.) for all amino acids except the C-terminal acid. The usual
nomenclature is the three letters or the one letter abbreviation for the amino acid
e.g., the above tripeptide is named as Ala-Gly-Phe or A-G-F.
Polypeptides are amphoteric because of the presence of terminal ammonium and
carboxylate ions as well as the ionized side chains of amino acid residues. Therefore,
they can be titrated as acids or bases and have an isolectric point at which they are
frequently least soluble and have the greatest tendency to aggregate.
The functions of proteins are important and valued in bio systems. However the
smaller peptides also have important functions though their total content in tissues is
small compared to proteins. Some of them are very potent. Most of the toxins
(poisonous substances) in animal venoms and in plant sources are polypeptides.
Minute amount of some oligopeptides with as few as three modified amino acid
residues are effective as hormones. A derivative of dipeptide aspartylphenylalanine
methyl ester (aspartame) is 160 times as sweet as sucrose and is used as a sugar
substitute.
Structure of Proteins
Proteins are biopolymers containing a large number of amino acids joined to each
other by peptide linkages having three dimensional structures. They are classified
into two major types on the basis of molecular shape as follows:
Fibrous Proteins
These have thread like molecules, which tend to lie side by side to form fibers. The
molecules are held together by hydrogen bonds. These are generally insoluble in
water. These proteins serve as the chief structural material of animal tissues. The
fibrous proteins e.g., fibroin in silk, collagen in tendons and -keratins in skin, hair,
nails, feathers etc., have large helical content and have a rod like rigid shape and are
insoluble in water. The structure of collagen triple helix is shown in the figure below.

Globular Proteins
In such proteins, molecules are folded into compact units that often approach
spheroidal shapes. The inter-molecular forces in them are weak due to the smaller
area of contact between the molecules. Haemoglobin is an example wherein the
polypeptide chains consist partly of helical sections which are folded about the
random cuts to give it a spherical shape. These are soluble in water. Globular
proteins function as,
Enzyme which catalyze all biological reactions
Regulate metabolic processes. For example, insulin maintains blood sugar
level and
Act as antibodies, which protect the body from the effect of invading species.
The structure of proteins is a complex one and can be divided into 4 parts. They are
primary, secondary, tertiary and quaternary structures.
Primary Structure of Proteins
The covalent structure of a protein responsible for its functioning is called its primary
structure. It shows the way various amino acids are held together in protein
molecule by peptide bonds to form chains. As all proteins on hydrolysis give -
amino acids, this shows that these are polypeptides and have a structure shown
below.

A protein containing a total of 100 amino acids residues is a very small protein, yet
20 different amino acids can be combined at one time in (20)
100
different ways!
Proteins may have 1 or more polypeptide chains. Each polypeptide in a protein has
amino acids linked with each other in a specific sequence and it is this sequence of
amino acids that is said to be the primary structure of that protein. The differences in
chemical and biological properties of various proteins and peptides arise due to the
difference in their primary structure.
Secondary Structure of Proteins
The primary structure of a protein gives only the nature of linkages of -amino acids
in a protein chain. However, it gives no idea about the shape or the conformation of
the molecule. The secondary structure explains this and is related to the
arrangement of polypeptide chains that maybe linear or may have a folding of the
polypeptide chain. Two different types of secondary structures are observed.
-Helix Structure
The folding of peptide chains which gives shape to this structure arises due to the
hydrogen bonding between and -NH groups. The formation of hydrogen bonds
causes the peptide chains to coil up into a spiral structure called the -helix similar
to a corkscrew. The helical structure of proteins was postulated by Linus Pauling in
1951, based purely on theoretical consideration but has since been confirmed by X-
ray diffraction. Examples of proteins having -helical structure are the fibrous
proteins such as those present in hair and wool. In the helix structure, the -NH group
of one unit is linked to -CO- group of the third unit by hydrogen bonding. The
hydrogen bonds hold the helix in position. On an average, there are three to four -
amino acids in each turn of the helix. The figure drawn below shows resonance
between different peptides linkages to understand the nature of the peptide bond.

Due to the partial double bond character of the C-N bond in peptide linkage, the
amide part (-CO-NH-) is planar and rigid i.e., no free rotation about this bond is
possible.

- Pleated Structure
When hydrogen bonds are formed between amide groups of two different chains, a
different type of secondary structure is obtained. It is known as -sheet or pleated
sheet structure. This structure is formed by side by side arrangement of different
polypeptide chains which are held together by intermolecular hydrogen bonds
between groups of neighbouring chains.
This type of structure is found in the -keratins such as silk.


Tertiary structure of Proteins
The three dimensional structure called the tertiary structure of a protein shows
further folding of the secondary structure. It coils and folds in such a way that the
hydrophobic side chains are held interior and the hydrophilic groups are held outside.
This arrangement gives stability to the molecule. The tertiary structure is a compact
structure and maintained by hydrogen bonds, disulfide bonds, ionic bonds and
hydrophobic interactions. This structure brings distant amino acid side chains nearer.

Quaternary Structure of Proteins
Several Complex proteins are formed from two or more -helix structures. The
spatial arrangement of these -helix structures with respect to each other is known
as quaternary structure. It indicates the way in which these -helix structures are
associated with each other in a complex protein.
The primary, secondary and tertiary and quaternary levels are given in figure below.

The primary, secondary and tertiary and quaternary structure of haemoglobin is also
given below.

Denaturation of Proteins
At normal temperature and pH, proteins found in a biological system will take a
shape, which is energetically most stable. This shape is specific. It depends upon the
amino acid sequence and is called the native state of protein.
When the native form of protein structure undergoes drastic changes it gets
disorganized. This state is called denaturation. It is caused by some physical and
chemical agents. Denaturation causes loss in biological activity of protein. The
peptide bonds in the primary structure are not hydrolyzed, but helical structure of
the protein is lost. Protein is soluble in water but after denaturation it is insoluble and
easily digested.
Denaturation is usually an irreversible process, but sometimes it is reversible. The
coagulation of egg white on boiling of egg protein is an example of irreversible
protein denaturation. The reversible process is called the reverse of denaturation i.e.,
renaturation. This is when the disruptive agent is removed and the protein recovers
its original physical and chemical properties and biological activity.


Enzymes
Enzymes are protein molecules catalyzing biochemical reactions in an
organism. They are polypeptides of amino acids that increase the rate of the
reaction to a great extent, without undergoing any change themselves.
Enzymes are the biocatalysts of life. They are crucial in allowing all major
metabolic reactions in living bodies to proceed at a rate optimal for its well
being. For instance, Enzymes react on our food instantly to break it down
into simple molecules in a very short span of time; without digestive
enzymes, it would take about 50 years to digest a single meal!
Enzymes are synthesized by living cells. They are simple or conjugate protein
and specific in action. An enzyme facilitates a biochemical reaction by
providing alternative lower activation energy pathways (similar to the action
of chemical catalysts), thereby increasing the rate of reaction. For example,
activation energy for acid hydrolysis of sucrose is 6.22 kJ mol
-1
, while the
activation energy is only 2.15 kJ mol
-1
when hydrolyzed by the enzyme,
sucrase.
Enzymes can be broadly categorized as:
Intracellular enzymes: these are functional within cells where they are
synthesized. Such enzymes catalyze all the hydrolysis of fats, sugars and
proteins within a cell. Enzymes also provide energy to the cell for carrying
out necessary functions by a series of oxidation and reduction reactions.
Extra cellular enzymes: those that are active outside the cell (all the
digestive enzymes belong to this group).
Enzymes being proteins have a colloidal nature and often get inactivated
during reactions. They have to be constantly replaced by synthesis in the
body.
At present about 3000 enzymes are recognized of which about 10% i.e., 300
enzymes are commercially available. All enzymes are classified into six
classes by International Union of Biochemistry (IUB). Each class represents
the general type of reaction brought about by the enzymes in its class. The
prescribed order of various classes is:
Oxidoreductases: enzymes involved in oxidation-reduction reactions.
Transferases: enzymes that catalyze the transfer of functional groups.
Hydrolases: enzymes that bring about hydrolysis of various
compounds.
Lyases: enzymes specialized in the addition or removal of water,
ammonia, CO
2
etc.
Isomerases: enzymes involved in all the isomerization reaction.
Ligases: enzymes catalyzing the synthetic reactions where two
molecules are joined together and ATP is used.
Many enzymes work with certain non-protein molecules or factors to carry
out and optimize their activity. These may be organic molecules or inorganic
ions. The full functional enzyme is referred to as Holoenzyme. In general, the
protein part is called 'apoenzyme' and the no-protein part is called prosthetic
group. The prosthetic group that is covalently attached with the enzyme is
known as cofactor. These cannot be easily removed.


The prosthetic groups which get attached to the enzyme at the time of
reaction are known as coenzymes. These are usually organic molecules that
have low molecular weight, are loosely held, and can be easily removed.
Coenzymes are non-protein in nature and usually derived from water soluble
B-complex vitamins like thiamine, riboflavin, niacin etc.
The substance on which an enzyme acts is called a substrate. It undergoes a
chemical reaction due to the catalytic action of an enzyme. The substrate
molecules are relatively much smaller in size compared to an enzyme
molecule.

Mechanism of Enzyme Action
Enzymes can increase reaction rates by up to ten million times when
compared to those of uncatalyzed reactions. Accordingly, enzymes are
needed only in small quantities for the progress of a reaction.
For any chemical reaction to occur the atoms or molecules of the reactants
must posses enough activation energy in order to react and form products;
that is, they have to be in an activated state. As was mentioned earlier,
enzymes lower the energy barrier or activation energy of reactants, thereby
enabling the reaction to proceed faster at normal body temperature.
Only a small area on the surface of the enzyme called the active site is
directly involved in binding the substrate for catalytic activity. The active site
on a given enzyme is so shaped that only a particular substrate can fit into it.
When the enzyme binds the substrate in the active site the realization of the
activated state is achieved very quickly. The enzyme acts on the substrate
and forms an enzyme-substrate complex. Once this occurs, a catalytic
chemical reaction occurs to form the enzyme-product complex (EP). The
formation of the product (P) occurs at this stage. The product is released
after the catalysis, and the enzyme is once again available for reuse.
The enzymatic reaction proceeds through four stages.
Classification according to the nature of carbonyl group.
Formation of complex between enzyme and substrate (ES)
Conversion of this complex to an enzyme-intermediate complex (EI)
Further conversion to a complex between enzyme and product (EP)
Dissociation of the enzyme - product complex, leaving the enzyme
unchanged.

Functions of Enzymes
Enzymes control several metabolic pathways and are highly specific in their
action.
Enzymes like invertase, zymase and maltase are used in manufacture
of alcoholic drinks.
Some enzymes are used as therapeutic agents e.g., streptokinase is
used to dissolve blood clots. Asparginase is used for treatment of
leukemia.
As the activity of enzyme decreases, the temperature of the body also
decreases.
Enzymes enhance the rate of reaction through acid-base catalysis and
covalent catalysis.
Estimation of serum enzymes helps in the right diagnosis of a
particular disease.
Deficiency symptoms
Deficiency of some enzymes causes diseases like albinism and phenyl ketone
urea in individuals.
Homopolysaccharides (homolycans) - one type of monosaccharide
Glucans (of glucose monomers) - e.g., Starch, Glycogen, Cellulose, Chitin
Galactans (of galactose monomers) - e.g., Agar Pectin Mannans (of
mannose monomers) - e.g., Yeast mannans Xylans (of xylan monomers) -
e.g., Hemicellulose xylan Fructans (of fructose monomers) - e.g., Inulin.
Heteropolysaccharides (heteroglycans) - two types of monosaccharides
Albinism is caused due to the deficiency of enzyme tyrosinase.
Phenyl ketone urea is caused due to the deficiency of enzyme
phenylalanine hydroxylase.


Vitamins
Vitamins are organic compounds required in the diet in small amounts to
perform specific biological functions for normal maintenance of optimum
growth and health of the organism. The bacterium E.coli does not require any
vitamin, as it can synthesize all of them. Plants can synthesize cell vitamins
whereas only a few are synthesized in animals and hence need to be supplied
in the foods. It is believed that during the course of evolution, the ability to
synthesize vitamins was lost. Hence, the higher organisms have to obtain
them from diet. Vitamins are required in small amounts, since their
degradation is relatively slow.
There are about 15 vitamins essential for humans. They are classified as fat-
soluble (A, D, E and K) and water-soluble (C and B-group) vitamins. Vitamin
D may be supplied through food or may be produced in the skin by
irradiation of sterols with sunlight (UV light). Human body can synthesize
Vitamin A from carotene and some members of Vitamin B complex and
Vitamin K are synthesized by microorganisms present in intestinal tract.
All cells of the body can store vitamins to some extent. However most of the
vitamins have been synthesized and are available commercially. They are
effective when taken orally.
Classification of Vitamins
Based on their solubility Vitamins are classed into two majors groups.
Fat Soluble Vitamins
The four vitamins, namely vitamin A, D, E, and K are known as fat or lipid
soluble. These vitamins are soluble in fats and oils and also the fat solvents
(alcohol, acetone etc.). Their availability in the diet, absorption and transport
are associated with fat. Fat-soluble vitamins can be stored in liver and
adipose tissue; they and are not readily excreted in urine and are not
absorbed in the body unless fat digestion and absorption proceed normally.
Among all the four vitamins only Vitamin K has a specific coenzyme function.
Fat soluble vitamins are made up of one or more carbon units and hence
they are called isoprenoid compounds. Their deficiency can cause
malabsorptive disease, while the excess intake of these vitamins may cause
hyper vitaminoses.
Water Soluble Vitamins
The water-soluble vitamins are a heterogeneous group of compounds since
they differ chemically from each other. The only common character shared
by them is their solubility in water. They are again divided into B complex
vitamins and non-B complex vitamins. B-complex vitamins are - thiamine
(B
1
), riboflavine (B
2
), niacin (B
3
), pyridoxine (B
6
), biotin (B
7
), pantothenic
acid, Folic acid and Cyanocobalamine (B
12
). Vitamin C is the non-B complex
vitamin.
These vitamins are not stored in the body (except B
12
). Most of these
vitamins are readily excreted in urine and they are toxic to the body. Water-
soluble vitamins must be continuously supplied in the diet. The biochemical
reactions of these vitamins are through co-enzymes. Generally, the common
vitamin deficiencies due to them are multiple rather than individual and
include dermatitis, glossitis, diarrhoea, depression, etc.
Important vitamins for humans are:
Vitamin A
Vitamin D
Vitamin E
Vitamin K
Vitamin C (Ascorbic acid)
Vitamin B
1
(Thiamine)
Vitamin B
2
(Riboflavin)
Vitamin B
6
(Pyridoxine)
Vitamin B
12
(Cobalamin)
Vitamin A
This is a fat soluble vitamin which is present mostly in animals. Its
provitamin carotenes are found in plants. Vitamin A is necessary for vision
and proper growth. It is necessary for maintenance of proper immune
system to fight various infections. Cholesterol synthesis requires vitamin A.
The carotenoids act as antioxidants and reduce risk of cancers.
Sources:
The animal sources are liver, kidney, egg, milk and its products like
cheese and butter.
Fish is very rich source of vitamin A.
Dark green vegetables and fruits are good sources of carotenes e.g.,
carrots, spinach, amaranthus, papaya, pumpkins, etc.
Deficiency Diseases: The deficiency of vitamin A is related to eyes, skin and
growth. The major deficiency manifestations are related to eyes. It causes
xerophthalmia i.e., hardening of cornea of eye. It also results in 'night
blindness' a deficiency caused in many individuals. Affected individuals have
difficulty to see in dim light. This is the earliest stage of deficiency; if this
prolongs it causes the destruction of cornea, causing total blindness. This is
called Keratomalacia.
The other manifestations caused due to the deficiency are growth
retardation, dryness of skin, bacterial infections of urinary tract, etc.
Vitamin D
This is also a fat soluble vitamin. Ergo calciferol and cholecalciferol are the
provitamins of vitamin D. Ergocalciferol is vitamin D
2
formed from ergosterol.
Cholecalciferol is vitamin D
3
found in animals. Vitamin D is stored in liver and
other tissues. Calcitrol is the biologically active form of vitamin D. It is
produced in kidney. It acts on intestines and bones.
Sources: Fish, fish liver oils, egg yolk are the rich sources of vitamin D.
Exposure of skin to sunlight is a way through which vitamin D is provided to
the body.
Deficiency Symptoms: The deficiency of this vitamin leads to
demineralization of bones. It causes rickets in children. Rickets is
characterized by bone deformities. It results in soft and liable bones and
delays in teeth formation. In adults, vitamin D deficiency causes
osteomalacia a condition where bones become softer and cause fractures.
Higher consumption of vitamin D causes hyper vitaminosis D. This leads to
formation of stones in kidneys. More consumption of vitamin D causes loss of
appetite, increased thirst, etc.
Vitamin E
This vitamin is named as tocopherol. Nearly about 8 tocopherols are
identified - , , etc. Among these -tocopherol is most active. Vitamin E is
stored in adipose tissue, liver and muscle. It acts as a scavenger and is
essential for membrane structure, cellular respiration and storage of creatine
in skeletal muscle. It protects liver from being damaged.
Sources: Vegetable oils are the rich sources of vitamin E. Sunflower oil,
wheat germ oil, cotton seed oil and corn oil are the good sources of vitamin
E. It is also present in small amounts in meat, milk, butter and eggs.
Deficiency diseases: The deficiency of this vitamin occurs mainly in animals.
It causes sterility, megaloblastic anaemia. It also causes changes in central
nervous system. Compared with animals, deficiency of vitamin E is not
severe in humans. In humans it causes increased fragility, minor neurological
disorders. Major defect is observed in fat absorption and transport.

Vitamin K
This is the only fat soluble vitamin which has a coenzyme function. It exists
in different forms - K
1
, K
2
, and K
3
. The main function of vitamin K is with
blood clotting process. It is required for carboxylation of glutamic acid
residues. Vitamin K acts as coenzyme in this carboxylation process. It also
involves in electron transport chain and oxidative phosphorylation. Vitamin K
1

called phylloquinone is found in plants. Vitamin K
2
called menaquinone is
found in intestinal bacteria and some animals. K
3
is called menadione which
is a synthetic form.
Sources: Good sources of vitamin K are green vegetables, cabbage,
cauliflower, tomatoes and spinach. It is also present in meat, liver and dairy
products.
Deficiency Diseases: The deficiency of vitamin K effects blood clotting
mechanism. The blood clotting time increases and the individual bleeds
heavily even for minor injuries. Deficiency of vitamin K leads to lack of
prothrombin.
Excess administration of vitamin K causes jaundice in infants. Heparin acts as
anticoagulant.
Vitamin C
This is a water soluble non-B complex vitamin known as ascorbic acid. Man
cannot synthesize ascorbic acid due to the lack of an enzyme while animals
can synthesize it with gluconolactone oxidase. Intake of vitamin C has a
curative impact on common cold. It is also helpful in wound healing process
and bone formation. Vitamin C is also useful in tryptophan metabolism,
tyrosine metabolism, fatty acid metabolism and cholesterol metabolism.
Vitamin C reduces cataract formation and also prevents chronic diseases.
Sources: Rich sources are citrus fruits and gooseberry. Good sources are
guava, green vegetables, tomatoes and potatoes. Milk is a poor source of
ascorbic acid.
Deficiency Diseases: The disease caused due to the deficiency of vitamin C is
scurvy. This disease causes spongy and sore gums, loose teeth, fragile blood
vessels, swollen joints, etc. The main characteristic of this disease is
anaemia.
Intake of mega doses of vitamin C leads to urinary tract infections. Intake of
proper doses of vitamin C cures common cold.
Thiamine (Vitamin BB
1
)
This is a water soluble vitamin with a specific coenzyme Thiamine
pyrophosphate (TPP). This coenzyme TPP function is connected to
carbohydrate metabolism. Thiamine is non toxic. The requirement of
thiamine in a body depends on the intake of carbohydrate. Many enzymatic
reactions in carbohydrate metabolism are dependant on TPP. For example,
pyruvate dehydrogenase, transketolase, ketoglutarate dehydrogenase, etc.
Sources: Good sources are cereals, pulses, nuts and yeast. Thiamine is
mostly found in outer layer of cereals. It is also found in pork, liver, heart,
kidney, milk, etc.
Deficiency Diseases: The disease caused due to the deficiency of thiamine is
beri-beri. Early symptoms of this deficiency are weakness, constipation,
mental depression, loss of appetite, etc. Two types of Beri-Beri are observed.
They are dry beri beri, wet beri-beri. Dry beri-beri causes neurological
manifestations. Muscles become weak and walking becomes difficult and the
individual become bed ridden. Wet beri-beri causes breathlessness and
palpitation. Heart becomes weak and death occurs due to heart failure.
Riboflavin (B
2
)
This is also a water soluble vitamin which helps in the oxidation - reduction
reactions through its coenzymes. The two coenzymes of this vitamin are
Flavin mononucleotide (FMN) and Flavin adenine dinucleotide (FAD).
Enzymes that use flavin coenzymes are called as flavo proteins. Flavo
proteins containing metal atoms are called as metallo flavo proteins.
Sources: Rich sources are milk and its products, meat, eggs, liver and
kidney. Cereals, fruits, vegetables and fish contain moderate amounts of
riboflavin.
Deficiency Diseases: The deficiency of this vitamin is uncommon and is
observed mostly in chronic alcoholics. The deficiency of this vitamin causes
Dermatitis, Glossitis and Cheilosis.
Intake of large doses of riboflavin does not affect the body. It is excreted in
faeces.
Niacin
This is also called as Nicotinic acid. The coenzymes are nicotinamide
dinucleotide (NAD) and nicotinamide dinucleotide phosphate (NADP). These
coenzymes participate in oxidation - reduction reactions and in almost all the
metabolisms.
Sources: Rich sources of Niacin are yeast, whole grains, cereals and pulses,
liver. Milk, fish, eggs and vegetables are the moderate sources of niacin.
Deficiency Diseases: The disease caused due to the deficiency of this vitamin
is pellagra. The symptoms of pellagra are dermatitis, diarrhoea, and
dementia. These are referred as three D's. If the patient is not treated it may
lead to death.
Dermatitis is observed on skin that is exposed to sunlight. Diarrhoea is in
form of loose stools with blood and mucus. Prolonged diarrhoea leads to
weight loss. Symptoms of dementia are anxiety, poor memory, etc.
Pyridoxine (B
6
)
Pyridoxine is a water soluble vitamin with pyridine derivatives. These are
pyridoxine, pyridoxal and pyridoxamine. Pyridoxine is a primary alcohol,
pyridoxal is an aldehyde and pyridoxamine is an amine form. Pyridoxine can
be converted to pyridoxal and pyridoxamine where as they cannot form
pyridoxine. Pyridoxal phosphate is the coenzyme of BB
6
. It participates in
reactions like transamination, deamination, condensation, etc.
Sources:Rich sources of vitamin B
6
are egg, fish, milk and meat. Wheat,
corn, cabbage, roots and tubers are some other sources of vitamin B
6
.
Deficiency Diseases: The deficiency of vitamin B
6
causes depression,
irritability, nervousness and mental confusion. Severe deficiency of this
vitamin causes convulsions and peripheral neuropathy. Demyelination of
neurons and decrease in haemoglobin levels are also observed due to this
vitamin deficiency.
Vitamin B
12
(Cyanocobalamin)
This is the only vitamin with a complex structure. The empirical formula of
vitamin B
12
is C
63
H
90
N
14
O
14
PCO. Vitamin BB
12
is also known as anti pernicious
anemia vitamin. This is stored in liver to meet the body requirements.
Sources: Rich sources are liver, kidney, milk, eggs, fish, pork and chicken.
Vitamin B
12
is synthesized in micro-organisms and hence BB
12
is found only in
animal foods and absent in plant foods.
Deficiency Diseases: The disease caused due to the deficiency is pernicious
anemia. Symptoms of this disease are low haemoglobin levels, decreased
number of erythrocytes and neurological manifestations. The deficiency of BB
12

also causes numbness and tingling of fingers and toes. If the deficiency is
severe it causes confusion, etc.
Functions of Vitamins in Biosystems
Vitamins are the important food factors required in diet. Different vitamins
are involved in different biochemical functions. They are required in very low
concentration and the daily requirement of any vitamin for any individual is
extremely small. The daily dose of any vitamin is not a fixed quantity but
varies according to size, age and rate of metabolism of the individual.
Youngsters need higher quantity of vitamins then elders and their
requirement increases when a person performs exercise. Growing children
and pregnant mothers need more quantity of vitamins in their diet.
A lack of one or more vitamins leads to characteristic of vitamin deficiency is
known as avitaminosis.


Nucleic acids
Nucleic acids are essential components of all cells. They play an essential role
in the transmission of hereditary characteristics and the biosynthesis of
specific proteins required by the organism. They are produced along with
proteins in the nucleus of every cell, upon hydrolysis of nucleoproteins, which
are the main constituents of genes and viruses. Hydrolysis of nucleic acids
produces phosphoric acid, a nitrogenous base, and a pentose carbohydrate.
Every living cell contains nucleoproteins; substances made up of proteins
combined with biopolymers of another kind called the nucleic acids. Nucleic
acids are the long chain bio-polymers with complex structure. They serve as
transmitters of genetic information. There are two types of nucleic acids they
are Deoxyribonucleic acid (DNA) and Ribonucleic acid (RNA). These nucleic
acids are built up by monomeric units called nucleotides and contain a
polyphosphate ester chain.
DNA is found in the nuclei of cells; it is the chemical basis of heredity and
may be regarded as the reserve bank of genetic information. DNA is
exclusively responsible for maintaining the identity of different species of
organisms over millions of years. Further every aspect of cellular function is
under the control of DNA. The DNA is organized into genes, the fundamental
units of genetic information. The genes control the protein synthesis through
the mediation of RNA, as shown below.
DNA RNA Protein
Besides being present in the nucleus of eukaryotic organisms, DNA is also
found in the mitochondria and chloroplasts. DNA in these organisms performs
specified functions with regard to protein synthesis.
RNA is found mainly in cytoplasm. It performs several functions, carried out
by three different types of RNAs.
Messenger RNA ('m' RNA) specifies the sequence of amino acids in the
protein synthesis (translation).
Ribosomal RNA ('r' RNA) is found in combination with proteins and is
associated with the structure and function of ribosomes, the factories of
protein synthesis.
Transfer RNA ('t' RNA) delivers the amino acids to ribosomes for
protein synthesis.
RNA as ribonucleoprotein participates in the post-transcriptional
modification of other RNAs.
RNA (not DNA) is the genetic material carrying hereditary information
in many viruses.
Both RNA and DNA are polymers of the monomeric units known as
nucleotides.
Composition
Nucleic acids are polymers of the monomeric units known as nucleotides.
Nucleotides contain a sugar and a heterocyclic nitrogenous base along with
phosphoric acid. Nucleotides are held by 3' and 5' phosphate bridges.
Nitrogenous bases are found in nucleotides are of two types. They are -
Purines and Pyrimidines.
Chemical Composition of Nucleic Acids
Nucleic acids are made up of three chemical components:
A nitrogen-containing base
A five-carbon sugar, and
A phosphate
General Structure of Nitrogen Bases:

Purine Bases

Pyrimidine Bases

Five-carbon Sugar

In nucleic acids sugars with five carbon monosaccharides are found. They are
D-ribose and deoxyribose. Deoxyribose differs from ribose is not having an -
OH on C
2
.
Nucleosides
The term nucleoside refers to base + sugar. Thus, the structure of nucleotide
can be said as nucleoside + phosphate. A pentose sugar added to a base
produces nucleoside. The bases in nucleic acids are adenine (A) and guanine
(G) derived from purine, and cystosine (C), thymine (T), and uracil (U) which
are derived from pyrimidine. The purine or pyrimidine bases are attached to
position 1 of pentoses through glycosidic linkages. If the sugar is ribose,
ribonucleosides are formed. In the same way if the sugar is deoxyribose,
deoxyribonucleosides are formed. Both the nucleosides differ with each other
in their bases. DNA contains the purine bases - adenine (A) and guanine (G)
and pyrimidine bases - Thymine (T) and cytosine (C). RNA has uracil (U) in
place of thymine (T).

Nucleotides
When a phosphate group is added to the nucleoside then it is called as
nucleotide. The carbons of sugars are represented with an associated prime
('). The bond between pentose and base is -N-glycosidic bond. N
9
of purine
ring binds with C
1
of pentose sugar. In pyrimidines the bond is in between N
1

of pyrimidine and C
1
of pentose. When a phosphate group is attached at 5'
position of a sugar then it is written as Adenosine 5'-monophosphate (AMP).
The nucleotides are abbreviated by three capital letters, preceded by d- in
case of deoxy series i.e.,
dAMP = deoxyadenosine monophosphate
ATP = adenosine triphosphate
UDP = Uridine diphosphate

Nucleotides are joined to the phosphate group by a phosphodiester linkage
between 5' and 3' carbon atom of a pentose sugar as shown below.

A nucleic acid chain is commonly abbreviated by a one letter code with 5' at
the end of the chain at the left e.g., a tetra nucleotide having A, C, G and T
bases from 5' and to 3' end is represented as ACGT. This tetra nucleotide is
drawn as,

Structure of Nucleic Acids
Structure of DNA
DNA is a polymer of deoxyribonucleotides (or simply deoxynucleotides). It is
composed of monomeric units namely deoxyadenylate (dAMP),
deoxyguanylate (dGMP), deoxycytidylate (dCMP), and deoxythymidylate
(dTMP) (or TMP since it is found only in DNA).
In higher cells, DNA is localized mainly in the nucleus within the
chromosome. A small amount of DNA is present in the cytoplasm also. It is
contained in the mitochondria and chloroplasts. DNA nucleotides contain the
'code' for specific amino acid sequences. It is the major source of genetic
information which is copied into RNA molecules (transcription). Proteins are
then synthesized in a process involving translation of RNA.
It was found that the base composition in DNA varied from one species to
other species but in all cases the amount of adenine was equal to that of
thymine (A=T)and the amounts of cytosine and guanine were also found to
be equal (G=C) therefore the total amount of purines was equal to the total
amounts of pyrimidines (A+G=C+T) However the AT/CG ratio varies between
species e.g., this ratio is 1.5 in man while in E coli it is 0.93.
DNA does not exist as a straight rod but its ends are covalently bonded to
give a closed circular or, a double stranded duplex molecule. This molecule is
a double helical structure made of deoxyribo nucleotides. This double helical
structure of DNA was proposed by Watson and Crick. Hence, it is known as
Watson and Crick model of DNA.
Watson and Crick Model of DNA
The double helix structure of DNA is similar to a twisted ladder. The three-
dimensional structure of DNA has been worked out with the help of its
diffraction patterns.
Salient Features
It is a double helix. Each helical polydeoxy ribonucleotide strand is a
right-handed helix wound in a double helix around the same central axis.
Each chain consists of alternate phosphate and sugar groups
connected through carbons 3 and 5 of the pentose molecules, and with the
bases attached to the pentose.
The two strands are antiparallel. The phosphodiester linkages of one of
these strands run in 5' to 3' direction while the other strand runs in 3' to 5'
direction. The bases are stacked inside the helix in planes perpendicular to
the helical axis.
These two strands are held together by hydrogen bonds. In addition to
hydrogen bonds, other forces e.g., hydrophobic interactions between
stacked bases are also responsible for stability and maintenance of double
helix.
Spatial considerations require that of the two linked bases one must be
a purine and the other a pyrimidine. The hydrogen bonding is very
specific. Adenine pairs only with thymine through hydrogen bonds and
guanine pairs only with cytosine through hydrogen bonds.
A-T pair has 2 hydrogen bonds while G-C pair has 3 hydrogen bonds.
Hence, is stronger than A=T.
The content of adenine is equal to the content of thymine and the
content of guanine is equal to the content of cytosine. This is Chargaff's
rule.
The two chains of DNA are said to be complementary to each other
since; given a sequence of bases on one chain the sequence on the other
chain can be determined.
The genetic information is present only on one strand known as
template strand.
The double helix structure contains major and minor grooves in which
proteins interact with DNA.

The diameter of double helix is 2 nm. The double helical structure repeats at
intervals of 3.4 nm (one complete turn) which corresponds to 10 base pairs.
The -conformation of DNA having the right handed helices is the most stable.
On heating the two strands of DNA separate from each other (known as
melting) and on cooling these again hybridize (annealing). The temperature
at which the two strands separately completely is known as its melting
temperature (T
m
) which is specific for each specific sequence.
Different Forms of DNA
Double helical structure exists in six different forms. They are A-DNA, B-DNA,
C-DNA, D-DNA, E-DNA and Z-DNA. Among these only 3 forms of DNA are
important. They are B-DNA, A-DNA and Z-DNA.
B-DNA
This is a double helical structure described above (Watson and Crick). It has
10 base pairs in each turn.
A-DNA
This is also a right handed helix. It has 11 base pairs per turn.
Z-DNA
This is a left handed helix. It has 12 base pairs per turn. The strands in this
form move in a 'zigzag' manner and hence it is called as Z-DNA.
Structure of RNA
RNA is also present in nucleus as well as cytoplasm. RNA forms long thread-
like molecules composed a single stranded structure made of ribonucleotides.
The chains fold back to form sections of double chains through hydrogen
bonding. RNA contains the pyrimidine uracil instead of thymine in DNA. Three
different varieties of RNA exist with widely different molecular weights.
The transfer RNA ('t' RNA)
Transfer RNA (soluble RNA) molecule contains 71 - 80 nucleotides (mostly
75) with a molecular weight of about 25,000. There are at least 20 species of
tRNAs corresponding to 20 amino acids present in protein structure.
The messenger RNA ('m'RNA)
This type is synthesized in the nucleus (in eukaryotes) as heterogeneous
nuclear RNA (hnRNA); hnRNA on processing liberates the functional mRNA,
which enters the cytoplasm to participate in protein synthesis, mRNA has
high molecular weight with short half-life.
The ribosomal RNA ('r' RNA)
The ribosomes are the factories of protein synthesis. They are composed of
two major nucleoprotein complexes - 60S subunit and 40S subunit. The
function of rRNAs in ribosomes is not clearly known. It is believed that they
play a significant role in the binding of mRNA to ribosomes and protein
synthesis.
Biological Functions of Nucleic Acids
The nucleic acids serve two important functions: duplication and protein
synthesis. Nucleic acids control heredity on a molecular level. DNA is the key
to cellular reproduction, for it carries information to form proteins and
enzymes and a duplicate copy of it. RNA is the substance by which the
information contained in the DNA is handed down from cell-to-cell and is
used in the formation of proteins.
Duplication
The genetic information for the cell is stored in the sequence of the bases A,
T, G, and C in the DNA molecule. When a cell divides, the parent DNA has
two complementary strands, which unwinds by breaking hydrogen bonds. In
this process, the two chains of DNA helix unwind and each chain serves as a
template for the duplication of a new chain. DNA replication follows the base
pairing rules by which A pairs with T and G pairs with C. Thus each daughter
molecule is an exact replication of the parent molecule. These daughter
molecules contain one parental strand and one new strand. Hence, this is
known as semi conservative replication.
Protein Synthesis
Another important function of nucleic acids is the protein synthesis in the
cell. Actually, the proteins are synthesized by various RNA molecules in the
cell but the message for the synthesis of a particular protein is present in
DNA. The hereditary information of the organism in DNA is coded in the form
of a sequence of bases along the polynucleotide chain. The DNA preserves
this information and uses it by 3 processes called,
Replication
Transcription
Translation
These concepts constitute the central dogma of molecular biology and are
summarized by Francis Crick in the following diagram.

Translation is unidirectional but transcription can sometimes be reversed i.e.,
RNA is copied into DNA. This reverse transcription occurs during life cycle of
some retroviruses.
Thus one can infer that base sequence in DNA indirectly contains the
sequence of amino acids in the protein. Since protein molecule can contain a
maximum of 20 different types of amino acids, it is like a large sentence
written in a language of 20 letters, but the hereditary message is written in a
language of only 4 letters: it is written in a code with each word of 3 letters
(triplet codon) standing for a particular amino acid.


Summary
Biomolecules are complex organic molecules which build up living
organisms and form the basis of life.
Organic compounds such as amino acids, nucleotides and
monosaccharides, serve as the monomeric units or building blocks of
biomolecules.
Biochemistry is the branch of chemistry which deals with the study of
chemical composition and structure of living organism and chemical
changes take place in them.
Carbohydrates are polyhydroxy aldehydes or ketones or the
compounds which can produce them on hydrolysis. They are broadly
classified into three groups - monosaccharides, oligosaccharides and
polysaccharides.
Monosaccharides are held together by glycosidic linkages to form
disaccharides or polysaccharides.
Glucose is the most important naturally occurring sugar which plays a
key role in release of energy to mammals.
D-glucose exists mainly in a six membered cyclic form in which two
carbon atoms are linked by an oxygen atom.
Glucose and fructose are important monosaccharides; sucrose,
maltose and lactose are important disaccharides; starch, cellulose and
glycogen are important polysaccharides.
Proteins are complex nitrogenous organic molecules that are essential
for growth and maintenance of life.
Proteins are polymers of about twenty different -amino acids which are
linked by strong, rigid and planar peptide bonds.
Proteins can have thread like molecules with a large helical content or
be folded in a globular structure. Proteins have are primary, secondary,
tertiary and quaternary structures.
Proteins can get denatured and be unable to function if their pH or
temperature conditions change.
Ten amino acids are called essential amino acids because they cannot
be synthesized by our body, hence must be provided through diet.
In zwitter ionic form, amino acids show amphoteric behaviour as they
react both with acids and bases.
Enzymes are biological catalysts produced by living cells that lower the
energy barrier or activation energy of reactants and speed up the
biochemical reactions. All enzymes are globular protein.
Enzymes are very specific and selective in their action. The enzymatic
reaction proceeds through formation of complex between enzyme and
substrate (ES) which further convert to an enzyme and product complex
(EP); dissociation of which gives the product.
Vitamins are accessory food factors required in the diet. They are
classified as fat soluble (A, D, E and K) and water soluble (? group and C).
Deficiency of vitamins leads to many diseases.
Nucleic acids are the polymers of nucleotides consisting of a base, a
pentose sugar and phosphate moiety.
Nucleic acids RNA and DNA are responsible for the transfer of
characters from parents to offsprings.
DNA stores the genetic information in the form of the sequence of
bases.
RNA is the substance by which the information contained in the DNA is
handed down from cell-to-cell and is used in the formation of proteins.

DNA contains a five carbon sugar molecule called 2-deoxyribose
whereas RNA contains ribose. Both DNA and RNA contain adenine, guanine
and cytosine as bases. The fourth base is different; it is thymine in DNA
and uracil in RNA.
DNA is a double helical structure while RNA is single stranded.
The process in which duplication of DNA takes place during cell division
is known as replication during which the genetic message is passed on to
the daughter nuclei.
During transcription one strand of DNA acts as a template on which a
complementary strand of RNA is synthesized.
The newly formed RNA dictates the synthesis of protein at the
ribosome. This process is known as translation.
Biomolecules are complex organic molecules which build up living
organisms and form the basis of life.
Organic compounds such as amino acids, nucleotides and
monosaccharides, serve as the monomeric units or building blocks of
biomolecules.
Biochemistry is the branch of chemistry which deals with the study of
chemical composition and structure of living organism and chemical
changes take place in them.
Carbohydrates are polyhydroxy aldehydes or ketones or the
compounds which can produce them on hydrolysis. They are broadly
classified into three groups - monosaccharides, oligosaccharides and
polysaccharides.
Monosaccharides are held together by glycosidic linkages to form
disaccharides or polysaccharides.
Glucose is the most important naturally occurring sugar which plays a
key role in release of energy to mammals.
D-glucose exists mainly in a six membered cyclic form in which two
carbon atoms are linked by an oxygen atom.
Glucose and fructose are important monosaccharides; sucrose,
maltose and lactose are important disaccharides; starch, cellulose and
glycogen are important polysaccharides.
Proteins are complex nitrogenous organic molecules that are essential
for growth and maintenance of life.
Proteins are polymers of about twenty different ?-amino acids which
are linked by strong, rigid and planar peptide bonds.
Proteins can have thread like molecules with a large helical content or
be folded in a globular structure. Proteins have are primary, secondary,
tertiary and quaternary structures.
Proteins can get denatured and be unable to function if their pH or
temperature conditions change.
Ten amino acids are called essential amino acids because they cannot
be synthesized by our body, hence must be provided through diet.
In zwitter ionic form, amino acids show amphoteric behaviour as they
react both with acids and bases.
Enzymes are biological catalysts produced by living cells that lower the
energy barrier or activation energy of reactants and speed up the
biochemical reactions. All enzymes are globular protein.
Enzymes are very specific and selective in their action. The enzymatic
reaction proceeds through formation of complex between enzyme and
substrate (ES) which further convert to an enzyme and product complex
(EP); dissociation of which gives the product.
Vitamins are accessory food factors required in the diet. They are
classified as fat soluble (A, D, E and K) and water soluble (? group and C).
Deficiency of vitamins leads to many diseases.
Nucleic acids are the polymers of nucleotides consisting of a base, a
pentose sugar and phosphate moiety.
Nucleic acids RNA and DNA are responsible for the transfer of
characters from parents to offsprings.
DNA stores the genetic information in the form of the sequence of
bases.
RNA is the substance by which the information contained in the DNA is
handed down from cell-to-cell and is used in the formation of proteins.
DNA contains a five carbon sugar molecule called 2-deoxyribose
whereas RNA contains ribose. Both DNA and RNA contain adenine, guanine
and cytosine as bases. The fourth base is different; it is thymine in DNA
and uracil in RNA.
DNA is a double helical structure while RNA is single stranded.
The process in which duplication of DNA takes place during cell division
is known as replication during which the genetic message is passed on to
the daughter nuclei.
During transcription one strand of DNA acts as a template on which a
complementary strand of RNA is synthesized.
The newly formed RNA dictates the synthesis of protein at the
ribosome. This process is known as translation.