Beruflich Dokumente
Kultur Dokumente
Chapter
31
Biomolecules
Glucose (C6 )
| |
COOH (CHOH )4 COOH H 2 O .
(CHOH )4 5 CH 3 COCl (CHOOCCH 3 )4 5 HCl
ZnCl 2
Saccharic acid (C6 )
Acetyl chloride
| | (c) Reaction with HCN
CH 2 OH CH 2 OOCCH 3 CH 2 OH(CHOH )4 CHO HCN
Glucose Glucose penta -acetate
CN
This shows that a molecule of glucose contains 5 – OH groups.
(b) Reaction with PCl CH 2 OH (CHOH )4 CH
5
Glucose cyanohydri n
CHO CHO OH
| | (d) Reaction with hydroxyl amine
CH 2 OH(CHOH )4 CHO NH 2 OH
(CHOH )4 5 PCl5 (CHCl )4 5 POCl3 5 HCl
CH 2 OH (CHOH )4 CH NOH H 2 O .
| | Glucose oxime
CH 2 OH CH 2 Cl (e) Reaction with Phenyl hydrazine (Fischer's mechanism) : When
Glucose Penta -chloroglucose warmed with excess of phenyl hydrazine, glucose first forms
(Glucose penta -chloride)
phenylhydrazone by condensation with – CHO group.
(c) Reaction with metallic hydroxides CHO +H NNHC H CH =NNHC H
C 6 H 11 O 5 — OH H O — Ca — OH
2 6 5
|
O |
6 5
Phenyl hydrazine
Glucose Calcium hydroxide CHOH CHOH
| |
C 6 H 11 O 5 — O — Ca — OH H 2 O (CHOH) Warm
Calcium glucosate
|
3
(CHOH) 3
CH OH |
Glucose behaves as a weak acid. Instead of Ca(OH )2 we can take 2
CH OH
Glucose
2
other metallic hydroxide like Ba(OH )2 , Sr (OH)2 , Cu(OH )2 etc to form Glucose phenyl hydrazone
The adjacent – CHOH group is then oxidised by a second molecule
glucosate which is soluble in water. of phenyl hydrazine.
(d) Formation of glycosides CH =NNHC H 6
CH = NNHC H
5 6 5
| |
C 6 H 11 O5 — OH H OCH 3 C 6 H 11 O5 OCH 3 H 2 O
HCl
C=O + C H NH + NH
α- and β-Methyl glucoside
CHOH +H NNHC H 2 6 5 6 5 2 3
CH O H | |
H OCH
(CHOH)
3
3
(CHOH) 3
|
3
C |
C
| | CH OH
2
CH OH 2
CH OH 2
| |
6 5
-Methyl glucoside |
2 6 5
C= NNHC H + H O
(ii) Reactions of carbonyl group (Aldehydic group) |
6 5 2
Na Hg |
CH 2 OH (CHOH )4 CHO 2 H CH OH
Glucose H 2O 2
CH OH 2
H – C – OH |
| | 2
H – C – OH
H – C – OH H – C – OH |
| | HO – C – H
3
CH OH 2
CH OH 2
| 4
CH OH 2
| |
HOCH — C
2
C — CHO Similarly a fresh aqueous solution of -glucose having specific
O rotation, [ ]D 19.7 o , on keeping (standing) gradually changes into the
Hydroxymethyl
same equilibrium mixutre (having, specific rotation 52.7 o ). So an
furfural
This on acid treatment gives laevulic acid aqueous solution of glucose shows a physical property, known as
(4) Uses mutarotation, i.e., a change in the value of specific rotation (muta=change;
rotation = specific rotation) is called mutarotation.
(i) In the preservation of fruits and preparation of jams and jellies.
(ii) In the preparation of confectionary and as a sweetening agent. H O H OH HO H
(iii) As a food for patients, invalids and children. 1 | 1
C 1
C C
(iv) In the form of calcium glucosate as medicine in treatment of | 2
| 2
| 2
CHOH
3
3
CHOH
(vi) As a raw material for alcoholic preparations. | 4
| 4 | 4
O
5
-D-
CH OHGlucose
6
CH OH 2 CH OH
content in blood. 2 2
D-Glucose -D-Glucose
(5) Test of glucose
(i) When heated in a dry test tube, it melts, turns brown and finally [] = + 52.5
D
o
[] = + 111 [] = + 19.7 D
o
D
o
black, giving a characteristic smell of burnt sugar. -Glucose ⇌ Open chain form ⇌ -Glucose
(ii) When warmed with a little conc. H 2 SO 4 , it leaves a charred 36% 0.02% 64%
(c) Fischer and Tollen’s proposed that the ring or the internal
residue of carbon. hemiacetal is formed between C 1 and C 4 . It means the ring is Furan
(iii) When it is boiled with dilute NaOH solution, it first turns type or 5-membered ring; this is called Furanose strucutre,
yellow and then brown.
However according to Haworth and Hirst the ring is formed
(iv) Molisch’s test : This is a general test for carbohydrates. Two or
three drops of alcoholic solution of -naphthol is added to 2mL of glucose between C 1 and C 5 . It means the ring is Pyran type or 6-membered ring,
solution. 1 mL of concentrated H 2 SO 4 is added carefully along the sides this is called Pyranose structure.
CH 2
4
4 3 5 3
CH — CH HC CH
|| 5
|| 2 ||6 ||2
CH CH HC CH
1 1
O O
Furan Pyran
Biomolecules 1431
(d) Haworth structure : The two forms of D-glucose are also shown
by Haworth projection formula which are given below,
CH OH CH OH
6 2 6 2
Table : 31.2 Comparison between glucose and fructose
5
O
5
It is present in abundance in fruits and hence is called fruit sugar. It With ethyl alcohol Almost insoluble More soluble
is also present in cane sugar and honey alongwith glucose in combined Oxidation
form. The polysaccharide inulin is a polymer of fructose an gives only
(a) With bromine water Gluconic acid No reaction
fructose on hydrolysis. Since naturally occurring fructose is laevorotatory, it
is also known as laevulose. (b) With nitric acid
CH OH 2 HOH C 2
OH Fructose gives reactions similar to glucose. The difference in
| properties is due to the fact that it contains a ketonic group while glucose
C= O CH OH C contains an aldehydic group.
2
| | |
HO – C – H C=O HO – C – H
or | Interconversions :
| |
(CHOH) H – C – OH O
H – C – OH |
3
(1) Chain Lengthening of Aldoses (Killiani-Fischer synthesis) : The
| |
CH OH conversion of an aldose to the next higher member involves the following
H – C – OH 2
H – C – OH
| steps :
|
CH OH CH 2
(i) Formation of a cyanohydrin.
- D- Fructose
2
D-Fructose
(ii) Hydrolysis of – CN to – COOH forming aldonic acid.
[]D = – 92° []D = – 21o
(iii) Conversion of aldonic acid into lactone by heating.
(iv) The lactone is finally reduced with sodium amalgam or sodium
OH CH OH 2
borohydride to give the higher aldose.
C
|
HO – C – H
|
H – C – OH O
|
H – C – OH
|
CH 2
1432 Biomolecules
CHO CN COOH The disaccharides yield on hydrolysis two monosaccharides. Those
| | | disaccharides which yield two hexoses on hydrolysis have a general formula
(CHOH) CHOH
|
3
HCN | H O/H
2
+
CHOH C12 H 22 O11 . The hexoses obtained on hydrolysis may be same or
CH OH (CHOH) 3 Ba(OH) | different.
2
| 2
Arabinose (CHOH)
CH OH 3
C12 H 22 O11
H 2O
C6 H 12 O6 C 6 H 12 O6
(Aldopentose) 2
| Sucrose
H Glucose Fructose
CH OH
O=C Lactose Glucose + Galactose
H 2O
2
Gluconic acid
| H
CHOH O=C–H
| | Maltose
H 2O
Glucose + Glucose
CHOH O CHOH H
heat | Na – Hg | The hydrolysis is done by dilute acids or enzymes. The enzymes
–H O CH in acid solution (CHOH) which bring hydrolysis of sucrose, lactose and maltose are invertase, lactase
|
2
3
|
CHOH CH OH and maltase, respectively. Out of the three disaccharides, sucrose (cane-
| 2
sugar) is the most important as it is an essential constituent of our diet.
CH OH Glucose
2
In disaccharides, the two monosaccharides are joined together by
(2) Chain Shortening of aldoses
-Lactone (Aldohexose)
glycoside linkage. A glycoside bond is formed when hydroxy group of the
(i) An aldose can be converted to the next lower member by Ruff hemiacetal carbon of one monosaccharide condenses with a hydroxy group
Degradation. of another monosaccharide giving – O– bond.
It involves two steps.
(1) Sucrose; Cane-sugar [C H O ] : It is our common table sugar. It is
CHO COOH
12 22 11
|
3
HO |
3
H O +Fe 3+
|
3
CH OH
2
CH OH
2 2
Aldopentose
2
O
sugar as it does not reduce Tollen’s
O = CH CH = NOH or Fehling’s reagent. Sucrose, on
| |
heating slowly and carefully, melts
1
CHOH CHOH OH
4
3 2 3 2
solidifies to pale yellow glassy mass 3
|
3
| | | O
CHO.COCH CHO H sugar. It is composed of -D-
|
3 AgOH
|
– HCN (CHOH
|
) 3
OH
2
| |
3 3
3 2
fructofuranose unit. These units are
Aldopentose
(3)CHConversion
O.COCH of an aldose toCHthe
2 OHisomeric Ketose Three steps are 3
2
joined by --glycosidic linkage 4
CH2OH 1
3
| |
CHOH C=NNHC H (a) As a sweetening agent for various food preparations, jams,
C H NHNH 2H O/H
6 5
| | +
6 5 2 2
syrups sweets, etc.
(CHOH) (Excess) (CHOH) (–2C H NHNH )
|
3
|
3
6 5 2
(b) In the manufacture of sucrose octa-acetate required to denature
CH OH 2
CH OH 2
alcohol, to make paper transparent and to make anhydrous adhesives.
Glucose Osazone (2) Inversion of cane-sugar : The hydrolysis of sucrose by boiling
HC=O CH OH with a mineral acid or by enzyme invertase, produces a mixture of equal
|
2
|
C=O molecules of D-glucose and D-fructose.
C=O 2H
| |
Zn/CH COOH (CHOH) C12 H 22 O11 H 2 O
H
C 6 H 12 O 6 C 6 H 12 O 6
(CHOH) 3 3
| | 3
Sucrose D- Glucose D- Fructose
(4) Conversion CH OH
of a ketose to the isomeric aldose (This mixture is laevorotatory)
CH OH 2
Fructose CHO
2
CHOH
| H /Ni CHOH [O] | glucose is 52 o and of D-fructose is 92 o . Therefore, the net specific
(CHOH) (CHOH)
2
(CHOH) H O + Fe 2 2
2+
|
3
CH OH |
3
CH OH 52 o 92 o
20 o
2 2
Fructose CH OH 2
Glucose 2
Disaccharides
Biomolecules 1433
Thus, in the process of hydrolysis of sucrose, the specific rotation is soluble in hot water, Amylopectin consists of D-glucose units from 300 –
changes from 66.5 to 20 , i.e., from dextro it becomes laevo and it 600. It is insoluble in water.
is said that inversion has taken place. The process of hydrolysis of sucrose is
thus termed as inversion of sugar and the hydrolysed mixture having equal CH2OH CH2OH CH2OH
molar quantities of D-glucose and D-fructose is called invert sugar. The
O O O
enzyme that brings the inversion is named as invertase.
Table : 31.3 Distinction between glucose and sucrose OH OH OH
O O O O
Test Glucose Sucrose
With conc. H SO in cold No effect Charring occurs and OH OH OH
2 4
n
turns black -1, 4-Glycoside bonds Repeating monomer
Molisch’s reagent Violet ring is Violet ring is formed Structure of amylose
formed CH2OH CH2OH
With NaOH Turns yellow No effect O O
With Tollen’s Solution Gives silver No effect OH OH
O O
mirror
With Fehling’s solution Gives red No effect OH
n
OH
precipitate of Repeating monomer
-1, 6-Glyoside bonds O
Cu O
2
On heating with phenyl Gives yellow No effect, i.e., does not CH2OH CH 2
CH2OH
hydrazine precipitate of form osazone O O O
glucosazone OH
O OH OH
Aqueous resorcinol + conc. No effect Reddish-brown O O O
HCl solution precipitate which OH
dissolves in ethanol. OH OH
Uses : Starch and its derivatives are used
-1, 4-Glycoside bonds Repeating monomer
(i) As the most valuableStructure
constituent of food as rice, bread, potato
of amylopectin
Polysaccharide (Starch and cellulose) and corn-flour, etc.
Polysaccharides are polymer of monosaccharide. The most important (ii) In the manufacture of glucose, dextrin and adhesives (starch
polysaccharides are starch and cellulose. They have a general formula paste).
(C 6 H 10 O 5 )n . Starch (Amylum) is most widely distributed in vegetable (iii) In paper and textile industry.
kingdom. It is found in the leaves, stems, fruits, roots and seeds. (iv) In calico printing as a thickening agent for colours.
Concentrated form of starch is present in wheat, corn, barley, rice, potatoes, (v) Nitro starch is used as an explosive.
nuts, etc. It is the most important food source of carbohydrates. (vi) Starch-acetate is a transparent gelatin like mass and is used
(1) Starch and its derivatives : Starch is a white amorphous mainly for making sweets.
substance with no taste or smell. When heated to a temperature between (2) Cellulose : It is found in all plants and so is the most abundant
of all carbohydrates. It is the material used to form cell walls and other
200 250 o C, it changes into dextrin. At higher temperature charring
structural features of the plants. Wood is about 50% cellulose and the rest
occurs. When boiled with dilute acid, starch ultimately yields glucose. is lignin. Cotton and paper are largely composed of cellulose.
(C 6 H 10 O 5 )n (C 6 H 10 O 5 )n1 Pure cellulose is obtained by successively treating cotton, wool, flax
Starch Dextrin or paper with dilute alkali, dilute HCl or HF . This treatment removes
mineral matter, water, alcohol and ether. Cellulose is left behind as a white
C12 H 22 O11 C 6 H 12 O 6 amorphous powder.
Maltose Glucose
Cellulose is insoluble in water and in most of the organic solvents. It
Both n and n1 , are unknown, but n is believed to be greater than decomposes on heating but does not melt. It dissolves in ammonical copper
n1 . hydroxide solution (Schwitzer’s reagent). Cellulose also dissolves in a
solution of zinc chloride in hydrochloric acid.
When treated with enzyme, diastase, it yields maltose.
When it is treated with concentrated H 2 SO 4 in cold, it slowly
2(C 6 H 10 O 5 )n nH 2 O nC12 H 22 O11 passes into solution. The solution when diluted with water, a starch like
Maltose
substance amyloid is precipitated and is called parchment paper. When
Starch solution gives a blue colour with a drop of iodine which boiled with dilute H 2 SO 4 , it is completely hydrolysed into D-glucose.
disappears on heating to 75 80 o C and reappears on cooling. The exact
(C 6 H 10 O 5 )n nH 2 O nC 6 H 12 O 6
chemical nature of starch varies from source to source. Even the starch Cellulose Glucose
obtained from same source consists of two fractions The cattle, goats and other ruminants can feed directly cellulose
(i) amylose and (grass, straw, etc.) as they have digestive enzymes (celluloses) capable of
(ii) amylopectin. hydrolysing cellulose into glucose. Man and many other mammals lack the
necessary enzymes in their digestive tract and thus cannot use cellulose as
Amylose is a linear polymer while amylopectin is a highly branched
food stuff.
polymer. Both are composed of -D-glucose units linked by glycosidic Cellulose is a straight chain polysaccharide composed of D-glucose
linkages. The number of D-glucose units in amylose range from 60 – 300. It units which are joined by B-glycosidic linkages between C-1 of one glucose
CH2OH H OH CH2OH
O O
H OH H H H H
H
O O O
OH H H H OH H
H
O
OH CH2OH H OH
1434 Biomolecules
unit and C-4 of the next glucose unit. The number of D-glucose units in NH 2
|
5
Ile / I
nitrates with camphor yield celluloid which is used in the manufacture of COOH
toys, decorative articles and photographic films. CH 3
(Essential)
(iii) In the form of cellulose acetate for the manufacture of rayon NH 2
(Essential) COOH
Test Glucose Sucrose Starch
HC CH
With iodine solution No effect No effect Blue 2 2
colour
HC CHCOOH
With Fehling’s Gives red precipitate No effect No effect Proline :
2
Pro / P
solution
With Tollen’s Gives silver mirror No effect No effect N
reagent
H
With phenyl Forms yellow No effect No effect
hydrazine osazone Amino acids with polar but neutral side chain :
Solubility in water Soluble Soluble Insoluble Three letter
Taste Sweet Sweet No taste Name / Structure symbol / One
letter code
Amino acids
Proteins are a class of biologically important compounds. They are H
crucial to virtually all processes in living systems. Some of them are |
hormones which serve as chemical messengers that coordinate certain N
biochemical activities. Some proteins serve to transport the substances through CH NH Trp / W
Tryptophan : 2
the organism. Proteins are also found in toxins (poisonous materials) as well as
in antibiotics. All the proteins are made up of many amino acid units linked C –CH –CH– COOH 2
together into a long chain. An amino acid is a bifunctional organic molecule (Essential)
that contains both a carboxyl group, –COOH, as well as an amine group, – NH 2
NH .
2
Serine : HO–CH –CH Ser / S
2
COOH
H Carboxyl group
|
NH 2
There are about 20 amino acids which make up the bio-proteins. Out of these 10 | Tyr / Y
Tyrosine : CH –CH–COOH
amino acids (non-essential) are synthesised by our bodies and rest are essential HO 2
in the diet (essential amino acids) and supplied to our bodies by food which we
take because they cannot be synthesised in the body. The -amino acids are NH 2
classified into the following four types and tasulabed as under, Cysteine : HS–CH –CH Cys / C
2
Table : 31.5
COOH
Amino acids with non polar side chain : NH 2
Glycine : CH Gly / G
2
Aspargine : C·CH ·CH Asn / N
COOH 2
O COOH
Biomolecules 1435
HN
2
NH 2
NH
NH 2
|
COOH NH 2
Alanine
Amino acids with basic side chains :
(iv) Streker synthesis
NH 2
Lysine : H N(CH ) CH
2 2 4 Lys / K H H H
| | |
COOH
(Essential) R C O R C OH R C NH 2
HCN NH 3
Aldehyde | |
NH NH 2
CN CN
Cyanohydri n Amino nitrile
Arginine : C·NH.(CH ) CH 2 3 Arg / R
HN (Essential) COOH H
2
| H2O
NH 2 R C NH 2 H+
|
C — CH — CH 2 COOH
HC - Amino acid
Histidine : COOH His / H
NH (v) From natural protein : Natural proteins are hydrolysed with dil.
N HCl or H 2 SO 4 at 250°C in an autoclave when a mixture of -amino acids
CH (Essential) is obtained. This mixture is esterified and the various esters are separated
by fractional distillation. The esters are then hydrolysed into respective -
(1) Methods of preparation of -amino acids amino acids.
(i) Amination of -halo acids (2) Physical properties
CH 3 CH COOH 2 NH 3 CH 3 CHCOOH NH 4 Cl (i) Amino acids are colourless, crystalline substances having sweet
| | taste. They melt with decomposition at higher temperature (more than
Br NH 2 200°C). They are soluble in water but insoluble in organic solvents.
- Bromo propionic acid - Amino propionic acid
(Alanine)
(ii) Except glycine, all the -amino acids are optically active and
Lab preparation of glycine
have an asymmetric carbon atom (-carbon atom). Hence, each of these
50 C
Cl.CH 2 COOH 3 NH 3 H 2 N .CH 2 COONH 4 NH 4 Cl amino acids can exist in two optical isomers. In proteins, however, only one
- Chloro acetic acid liquid Amm. salt of glycine isomer of each is commonly involved.
The ammonium salt so obtained is boiled with copper carbonate and (iii) Zwitter ion and isoelectric point : Since the NH 2 group is
cooled when blue colour needles of copper salt of glycine are obtained.
basic and – COOH group is acidic, in neutral solution it exists in an internal
2[H 2 N CH 2COONH 4 ] CuCO 3
Boiled
ionic form called a Zwitter ion where the proton of –COOH group is
transferred to the NH 2 group to form inner salt, also known as dipolar
(H 2 NCH 2COO )2 Cu (NH 4 )2 CO 3
Copper salt of glycine ion.
It is now dissolved in water and H 2 S is passed till whole of the R
|
copper precipitates as copper sulphide leaving glycine as the aqueous
H 2 N CHCOOH
In water
solution. - Amino acid
2 2 5
HCl
CO
COOH
+ CH NH COOH + C H OH
2 2 2 5
COOH Glycine
Phthalic acid
1436 Biomolecules
(3) Chemical properties : Amino acids are amphoteric in nature.
Depending on the pH of the solution, the amino acid can donate or accept
proton.
O O
|| H +
||
R C H C OH R C H C OH
| |
NH 2
(Neutral not isolated) N H3
pH 0
(Cation in fairlyacidic medium)
O O
|| ||
R C H C O R C H C O
| |
NH
N H3 2
pH 7 pH 11
(Zwitterion in neutral medium) (Anion in fairly basic solution)
CH 3 CH C H COOH CH 3 CH CHCOOH
heat The product formed by linking amino acid molecules through
( NH 3 )
| | Crotonic acid peptide linkages, CO NH , is called a peptide. Peptides are further
NH 2 H designated as di, tri, tetra or penta peptides accordingly as they contain two,
- Amino butyric acid
three, four or five amino acid molecules, same or different, joined together
(c) For and amino acids in the following fashions.
CH 2 CH 2 CH 2 CO CH 2 CH 2 CH 2 CO
heat O H O
|| | ||
| | ( H 2 O ) ( H 2 O )
H 2 N CH C OH H N CH C OH
NH H H O NH | |
- Amino butyric acid -Butyrolactam
R R
CH 2 C H 2 CH 2 CH 2 CO CH 2 CH 2 CH 2 CH 2 CO
heat O H O
|| | ||
| | ( H 2 O )
O H H 2 N CH C N CH C OH
NH H NH | |
- Amino valericacid - Valerolactum Peptide linkage
R (Dipeptide)
R
These lactams have stable five or six membered rings.
(ii) -amino acids show the reactions of –NH group, –COOH 2
When the number of amino molecules is large, the product is
groups and in which both the groups are involved. termed polypeptide which may be represented as,
NaOH
RCHNH COONa 2
Sodium salt
C H OH +
2 5
H NCHCOOC H
Dry HCl 3 2 5
R AgOH
H NCH – COOC H
2 2 5
Ethyl ester
R
Decarboxylationn
H N – CH
Biomolecules 1437
O O (6) Classification of proteins : According to chemical composition,
|| || proteins are divided into two classes
H 2 N CH C NH C H C NH CH COOH
| | | (i) Simple proteins : Simple proteins are composed of chains of amino
R R R acid units only joined by peptide linkages. These proteins on hydrolysis yield only
n
(4) Composition : Composition of a protein varies with source. An mixture of amino acids. Examples are :
approximate composition is as follows : Egg albumin, serum globulins, glutenin in wheat, coryzenin in rice,
Carbon 50-53%; hydrogen 6-7%; oxygen 23-25%; nitrogen 16-17%; tissue globulin, etc.
Sulphur about 1%. Other elements may also be present, e.g., phosphorus (in (ii) Conjugated proteins : The molecules of conjugated proteins are
nucleoproteins), iodine (in thyroid proteins) and iron (in haemoglobin). composed of simple proteins and non protein material. The non-protein
material is called prosthetic group or cofactor. These proteins on hydrolysis
(5) Structure of proteins : The structure of proteins is very complex.
yield amino acids and non-protein material. Examples are
The primary structure of a protein refers to the number and sequence of
the amino acids in its polypeptide chains (discussed in the formation of Mucin in saliva (prosthetic group, carbohydrate), casein in milk
proteins). The primary structure is represented beginning with the amino (prosthetic group, phosphoric acid), haemoglobin in blood (prosthetic
group, iron pigment), etc.
acid whose amino group is free (the N-terminal end) and it forms the one
end of the chain. Free carboxyl group (C-terminal end) forms the other end According to molecular shape, proteins are divided into two types
of the chain. (i) Fibrous proteins : These are made up of polypeptide chains that
O O run parallel to the axis and are held together by strong hydrogen and
Left hand side Right hand side
|| || disulphide bonds. They can be stretched and contracted like a thread. These
H 2 N CH C NH C H C NH ... CH COOH are usually insoluble in water. Examples are : -keratin (hair, wool, silk and
| | |
One end R R R Other end nails); myosin (muscles); collagen (tendons, bones), etc.
(N-terminal end) (R, R, R …may be same or different) (C-terminal end) (ii) Globular proteins : These have more or less spherical shape
(compact structure). -helics are tightly held up by weak attractive forces
Side chains may have basic groups or acidic groups as NH 2 in
of various types: Hydrogen bonding, disulphide bridges, ionic or salt bridges.
lysine and –COOH in aspartic acid. Because of these acidic and basic side These are usually soluble in water. Examples are: Insulin, pepsin,
chains, there are positively and negatively charged centres. Though the haemoglobin, cytochromes, albumins, etc.
peptide linkage is stable, the reactivity is due to these charged centres in the
Proteins can also be classified on the basis of their function
side chains.
Primary structure tells us nothing about the shape or conformation Table : 31.6
of the molecule. Most of the bonds in protein molecules being single bonds Protein Function Examples
can assume infinite number of shapes due to free rotation about single
Enzymes Biological catalysts, vital Trypsin, pepsin.
bonds. However, it has been confirmed that each protein has only a single
to all living systems.
three dimensional conformation. The fixed configuration of a polypeptide
skeleton is referred to as the secondary structure of a protein. It gives Structural proteins Proteins that hold living Collagen.
information : systems together.
About the manner in which the protein chain is folded and bent; Harmones Act as messengers. Insulin.
About the nature of the bonds which stabilise this structure. Transport proteins Carry ions or molecules Haemoglobin.
Secondary structure of protein is mainly of two types from place to another in
the living system.
(i) -helix : This structure is formed when the chain of -amino
acids coils as a right handed screw (called -helix) because of the formation Protective proteins Destroy any foreign Gamma globulin.
(antibiotics) substance released into
of hydrogen bonds between amide groups of the same peptide chain, i.e.,
the living system.
NH group in one unit is linked to carbonyl oxygen of the third unit by
hydrogen bonding. This hydrogen bonding between different units is Toxins Poisonous in nature. Snake venom.
responsible for holding helix in a position. The side chains of these units
project outward from the coiled backbone. (7) General and physical characteristic of proteins
Such proteins are elastic, i.e., they can be stretched. On stretching (i) Most of them (except chromoproteins) are colourless, tasteless, and
weak hydrogen bonds break up and the peptide chain acts like a spring. The odourless. Many are amorphous but few are crystalline. They are nonvolatile and
hydrogen bonds are reformed on releasing the tension. Wool and hair have do not have a sharp melting point .
-helix structure. (ii) Most of them are insoluble in water and alcohol. But many of
(ii) -pleated sheet : A different type of secondary structure is them dissolve in salt solutions, dilute acids and alkalies. Some proteins such
possible when polypeptide chains are arranged side by side. The chains are as keratins (skin, hair and nails) are completely insoluble.
held together by a very large number of hydrogen bonds between C = O (iii) Protein molecules are very complex and possess very high
and NH of different chains. Thus, the chains are bonded together forming a molecular masses. They are hydrophilic colloids which cannot pass through
sheet. These sheets can slide over each other to form a three dimensional vegetable or animal membrane. On addition of sodium chloride, ammonium
structure called a beta pleated sheet. Silk has a beta pleated structure. sulphate magnesium sulphate, etc., some proteins are precipitated. The
Globular proteins possess tertiary structure. In general globular proteins precipitate can be filtered and redissolved in water.
are very tightly folded into a compact spherical form.
1438 Biomolecules
(iv) The solution of proteins are optically active. Most of them are (v) Nitroprusside test : Proteins containing –SH group give this test.
laevorotatory. The optical activity is due to the presence of asymmetric When sodium nitroprusside solution is added to proteins having –SH group,
carbon atoms in the constituent -amino acids. a violet colour is developed.
(v) Isoelectric point : Every protein has a characteristic isoelectric O
point at which its ionisation is minimum. Like amino acids, proteins, having |
H
C
charged groups ( N H 3 and COO ) at the ends of the peptide chain, are OH |
amphoteric in nature. In strong acid solution, protein molecule accepts a C + RCCOOH
proton while in strong basic solution it loses a proton. The pH at which the |
C OH
protein molecule has no net charge is called its isoelectric point. This NH
|
2
property can be used to separate proteins from mixture by electrophoresis. Amino acid
O
(vi) Denaturation : The structure of the natural proteins is
responsible for their biological activity. These structures are maintained by
Ninhydrin O OH
various attractive forces between different parts of the polypeptide chains.
The breaking of these forces by a physical or a chemical change makes the | |
proteins to lose all or part of their biological activity. This is called C C
denaturation of proteins. The denaturing of proteins can be done by adding C
chemicals such as acids, bases, organic solvents, heavy metal ions, or urea. It C=N–
|
can also be done with the help of heat and ultraviolet light. Denaturation C C
R
can be irreversible or reversible. In irreversible denaturation, the | |
denaturated protein does not return to its original shape. For example, the
O O
heating of white of an egg (water soluble) gives a hard and rubbery
insoluble mass. Violet complex
(vi) Molisch’s test : This test is given by those proteins which
(8) Chemical properties contain carbohydrate residue. On adding a few drops of alcoholic solution of
(i) Salt formation : Due to presence of both NH 2 and –COOH -naphthol and concentrated sulphuric acid to the protein solution, a violet
groups in proteins, they form salts with acids and bases. Casein is present ring is formed.
in milk as calcium salt. (vii) Hopkins-Cole test : On adding concentrated sulphuric acid
(ii) Hydrolysis : The simple proteins are hydrolysed by acids, alkalies down the side containing a solution of protein and glyoxalic acid, a violet
or enzymes to produce amino acids. Following steps are involved in the colour is developed.
hydrolysis and the final product is a mixture of amino acids. (10) Uses
Protein Proteose Peptone Polypeptide Simple peptide (i) Proteins constitute as essential part of our food. Meat, eggs, fish,
Mixture of amino acids cheese provide proteins to human beings.
(iii) Oxidation : Proteins are oxidised on burning and putrefaction. (ii) In textile : Casein (a milk protein) is used in the manufacture of
The products include amines, nitrogen, carbon dioxide and water. The bad artificial wool and silk.
smell from decaying dead animals is largely due to the formation of amines (iii) In the manufacture of amino acids : Amino acids, needed for
by bacterial oxidation of body proteins. medicinal use and feeding experiments, are prepared by hydrolysis of
(9) Test of proteins proteins.
(i) Biuret test : On adding a dilute solution of copper sulphate to (iv) In industry : Gelatin (protein) is used in food products, capsules
alkaline solution of protein, a violet colour is developed. This test is due to and photographic plates. Glue (protein) is used as adhesive and in sizing
the presence of peptide (–CO–NH–) linkage. paper. Leather is obtained by tanning the proteins of animal hides.
(ii) Xanthoproteic test : Some proteins give yellow colour with (v) In controlling body processes : Haemoglobin present in blood is
concentrated nitric acid (formation of yellow stains on fingers while working responsible for carrying oxygen and carbon dioxide. Harmones (proteins)
with nitric acid in laboratory). The formation of yellow colour is due to control various body processes.
reaction of nitric acid with benzenoid structures. Thus, when a protein
(vi) As enzymes : Reactions in living systems always occur with the
solution is warmed with nitric acid a yellow colour may be developed which
aid of substances called enzymes. Enzymes are proteins produced by living
turns orange on addition of NH 4 OH solution. systems and catalyse specific biological reactions.
(iii) Millon’s test : When millon’s reagent (mercurous and mercuric Important enzymes tabulated as under,
nitrate in nitric acid) is added to a protein solution, a white precipitate
which turns brick red on heating, may be formed. This test is given by
proteins which yield tyrosine on hydrolysis. This is due to presence of Table : 31.7
phenolic group.
Enzymes Reaction catalysed
(iv) Ninhydrin test : This test is given by all proteins. When a Urease Urea CO + NH
protein is boiled with a dilute solution of ninhydrin, a violet colour is 2 3
Nucleic acids
In every living cell there are found nucleo-proteins which are made
up of proteins and natural polymers of great biological importance called
nucleic acids.
Two types of nucleic acids are found in biological systems, these are
Deoxyribonucleic acid (DNA) and Ribonucleic acid (RNA)
The nucleic acid was first isolated by Friedrich Miescher in 1868 Both differ only at carbon atom 2 in the ring.
from the nuclei of pus cells and was named nuclein. The term nuclein was (iii) Phosphoric acid, H PO : Phosphoric acid forms esters to –OH groups
3 4
given by Altman. of the sugars to bind nucleotide segments together. A molecule called nucleoside
is formed by condensing a molecules of the base with the appropriate pentose.
(1) Composition : Nucleic acids like proteins and carbohydrates are
(i.e., Base + Sugar).
polymer. The simple units that make up the nucleic acid are called
nucleotides. Nucleotides are themselves composed of following three simple NH
molecules. N 2
N
(i) Nitrogenous base : These are heterocyclic organic compound having Adenine
two or more nitrogen atoms in ring skeleton. These are called bases because the N
lone pairs of electrons on the nitrogen atoms make them as Lewis bases. N
NH
| 2
O OH CH OH O N
6 6
2
1
4
– HO 4
HN or N1 5
N or N1 5 C 1
C 2
C C
2 3
;
2
N 4
N 3 4 H H
O N O HO N H H H H H
HO H H
H C C
2, 6 dihydroxy Cytosine (C) Cytosine (C) C 3 C2 3 2
Uracil (U)
RNA pyrimidine HO combined
A nucleotide results when the nucleoside OHwith phosphoric
OH HO OH Adenosine (nucleoside)
O acid mainly at carbon 5 of the pentose. (i.e., Base + Sugar + Phosphoric
Ribose
CH 3
CH 3 acid). NH
6 5 2
HN N1 N
or 2
3 4 OH N
O N HO N
H |
2, 6 dihydroxy 5
Thymine (T) HO — P — O — CH 2
O N N
DNA 5-methyl pyrimidine |
NH NH 4 1
2 2
O C C
CH OH
H H
2
N CH ; N
H H
3
N N C C
HO HO 3 2
5-Methyl cytosine 5-Hydroxy methyl cytosine
(b) Purine derivatives HO OH
This nucleotide is the building block
Nucleotide-adenosine of both DNA
5-phosphoric acidand RNA. The
NH 2
nucleic acids are condensation polymers of the nucleotide monomers and
N OH are formed by the creation of an ester linkage from phosphoric residue on
N N
N1 6
5
7 8 1
6 7 8 one nucleotide to the hydroxy group on carbon 3 in the pentose of the
2
CH ; 2
CH second nucleotide. The result is a very long chain possessing upto a billion
3
3 4 4 5
N 9 HN N 9
or so nucleotides units in DNA.
N 2
N
H H
Adenine (A) Guanine (G)
DNA, RNA DNA, RNA |
(ii) Five carbon sugar (Pentose) : In RNA, the sugar is ribose where
as in DNA, the sugar is deoxyribose. HO – P – O – Sugar – Base
| |
5
CH OH O OH O O
2
1 CHOH
4 1 |
C C 2 CHOH O HO – P – O – Sugar – Base
H H or 3 CHOH
| |
H H O O
C C 4 CH
3 2 |
HO OH 5 CH OH 2
HO – P – O – Sugar – Base
1440 Biomolecules
Deep groove
3.4 A°
minimize loss of body heat and also act as cushions to absorb mechanical N C
impacts. O –
O O–
–
C N
Another very important class of lipids are the phospholipids. These | | | HCC
are polar lipids and like the fats, are esters of glycerol. In this case, however, C CH
only two fatty acid molecules are esterified to glycerol, at the first and O –
— P~O– P~O—P—O— CH 2
O N N
second carbon atom. The remaining end position of the glycerol is esterified | | |
to a molecule of phosphoric acid, which in turn is also esterified to another O O O
alcohol. This gives a general structure.
H H
Point of cleavage to form H H
ADP
R
ATP
Hydrolysis
ADP Pi H = –30.93 kJ mol –1
| Adenosine
diphosphat eHO OH
O
| ADP
Hydrolysis
AMP 2 Pi H = –28.4 kJ mol –1
O = P – O – CH 2
O Adenosine
monophosph ate
| | |
ADP can change to ATP in the presence of inoraganic phosphate.
OH CH – O – C – R This process is called phosphorylation.
|
CH O – C – R ATP
2
|
The alcoholic compound linked to phosphoric group may be choline,
ethanol, amine, serine or inositol. The phosphateO groups forms a polar end, Gains
i.e., hydrophilic (water-attracting) and the two fatty acid chains constitute Doing work
the non-polar tail, i.e., hydrophobic (water repelling). This structure gives inorganic Catabolism
the phospholipids good emulsifying and membrane forming properties. phosphate
Fuels
1444 Biomolecules
(2) Proteins Proteases and Peptones
Pepsin/ HCl
Trypsin
(Stomach) Chemotryps in
Pancreatic juice
Digestion of food (Intestine)
Digestion is the process by which complex constituents of food are
broken down into simple molecules by a number of enzymes in mouth, Peptides Amino acids
Peptidases
(Intestine)
stomach and small intestine. The simple molecules thus formed are
absorbed into blood stream and reach various organs. (3) Fats Emulsified fat
Bile salts
Fatty acids
Lipases
Raw food may be taken as such or after cooking. It is chewed in the Pancreatic and
(From liver)
intestine juice
mouth and swallowed when it passes through a long passage in the body
called alimentary canal. During this passage it gets mixed with various Glycerol
enzymes in different parts of the alimentary canal. The carbohydrates, After digestion, there are present glucose, aminoacids, fatty acids
proteins and fats are converted into simpler forms which are then carried along with vitamins and mineral salts. Undigested food and secretions are
by blood to different parts of the body for utilization. Digestion of food can pushed forward into the rectum from where these are excreted.
be summarized in the following form Vitamins
(1) Polysaccharide Disaccharides
Amylase
In addition to air, water, carbohydrates, proteins, fats and mineral
Saliva (mouth);
Pancreatic juice salts, certain organic substances required for regulating some of the body
(Intestine)
processes and preventing certain diseases are called vitamins. These
compounds cannot be synthesised by an organism. On the basis of
Disaccharides (maltose, etc.) Glucose
Maltase
(Intestine) solubility, the vitamins are divided into two groups.
(1) Fat soluble; Vitamin A, D, E and K.
(2) Water soluble; Vitamin B and C.
Table : 31.9
Name Sources Functions Effects of defficiency
Water soluble vitamins
Vitamin B 1
Rice polishings, wheat flour, oat meal, Major component of co-enzyme co- Beri-beri, loss of appetite and vigour,
(Thiamine or Aneurin) eggs, yeast, meat, liver, etc. carboxylase required for constipation, weak heart beat, muscle
(C H N SOCl ) carbohydrate and amino acid atrophy, even paralysis.
12 18 4 2
metabolism.
Vitamin B or G 2
Cheese, eggs, yeast, tomatoes, green Combines with phosphoric acid to Cheilosis, digestive disorders, burning
(Riboflavin or Lactoflavin) vegetables, liver, meat, cereals, etc. form coenzyme FAD essential for sensations in skin and eyes, headache,
(C H N O ) oxidative metabolism. mental depession, scaly dermatitis at
17 20 4 6
Vitamin B or P-P 5
Fresh meat, liver, fish, cereals, milk, Active group in coenzyme NAD Pellagra, dermatitis, diarrhoea, demenia,
(Nicotinic acid or Niacin) pulses, yeast, etc. required for oxidative metabolism. muscle atrophy, inflammation of
C H NO (C H N–COOH) mucous membrane of gut.
6 5 2 5 4
Vitamin B 6
Milk, cereals, fish, meat, liver, yeast Important coenzyme required in Dermatitis, anaemia, convulsions, nausea,
(Pyridoxine or Adermin) synthesised by intestinal bacteria. protein and amino acid insomnia, vomiting, mental disorders,
(C H O N) metabolism. depressed appetite.
8 11 3
Vitamin H (Biotin) Yeast, vegetables, fruits, wheat, Essential for fat synthesis and Skin lesions, loss of appetite, weakness,
(C H N O S)
10 16 2 3
chocolate, eggs, groundnut energy production. hairfall, paralysis.
synthesised by intestinal bacteria.
Folic acid group Green vegetables, soyabean, yeast, Essential for synthesis of DNA and Retarded growth, anaemia.
kidneys, liver, synthesised by intestinal maturation of blood corpuscles.
bacteria.
Vitamin B 12
Meat, fish, liver, eggs, milk synthesised Required for chromosome Retarded growth, pernicious anaemia
(Cyanocobalamine) by intestinal bacteria. duplication and formation of blood
(C H O N PCo)
63 88 14 14
corpuscles.
Vitamin C Lemon, orange and other citrus fruits, Essential for formation of collagen, Wound-healing and growth retarded,
(Ascorbic acid) (C H O ) 6 8 6
tomatoes, green vegetables, potatoes, cartilage, bone, teeth, connective scurvy, breakdown of immune defence
carrots, pepper, etc. tissue and RBCs and for iron system, spongy and bleeding gums,
metabolism. fragile blood vessels and bones,
exhaustion, nervous breakdown, high
fever.
Fat soluble vitamins
Vitamin A Synthesised in cells of liver and Essential for synthesis of visual Xerophthalmia-keratini-zed conjunctive
(Retinol or Axerophthol) intestinal mucous membrane from pigments; growth and division of and opaque and soft cornea.
(C H O) carotenoid pigments found in milk, epithelial cells. Stratification and keratinization in
20 30
butter, kidneys, egg yolk, liver, fish oil, epithelia of skin, respiratory passages,
etc. urinary bladder, ureters and intestinal
mucosa, night-blindness, impaired
growth, glandular secretion and
reproduction.
Vitamin D Synthesised in skin cells in sunlight Regulates absorption of calcium Rickets with osteomalacia; soft and
Biomolecules 1445
(Ergocalciferol), (Sun shine from 7-dehydro-cholesterol also found and phosphorus in intestine, fragile teeth.
vitamin) CHO and 28 44
in butter, liver, kidneys, egg yolk, fish mineral deposition in bones and
cholecalciferol oil, etc. teeth.
Vitamin E group Green vegetables, oil, egg yolk, wheat, Essential for proper Sterility (impotency) and muscular
Tocopherols (, , ) (C G O ) animal tissues. spermatogenesis, pregnancy, atrophy.
29 50 2
lactation and muscular function.
Vitamin K (Phylloquinone) Carrots, lettuce, cabbage, tomatoes, Essential for synthesis of Haemorrhages, excessive bleeding in
(C H O )
31 46 2
liver, egg yolk, cheese; synthesized by prothrombin in liver, which is injury, poor coagulation of blood.
colon bacteria. required for blood clotting.
aldoses in ketoses are called anomers. Thus -D glucose and -D glucose
are anomers and so are -D fructose and -D fructose.
Monosaccharides which differ in configuration at a carbon atom
other than the anomeric carbon are called epimers. Thus glucose and
mannose which differ in configuration at C are called C epimers while2 2
epimers.
In amino acids –COO group acts as the base while N H 3 acts as
–
the acid.
Insulin is a protein harmone. It consists of 51 amino acids arranged
in two polypeptide chains containing 21 and 30 amino acids residues
respectively. The two peptide chains are held together by two cystine
disulphide cross links.
Certain enzymes are associated with coenzymes mostly derived
from vitamins for their biological activity.
Each segment of a DNA molecule that codes for a specific protein
or a polypeptide is called gene and the relationship between the
nucleotide triplet and the amino acids is called the genetic code.
Phospholipids are major constituents of cell walls.
The deficiency of essential amino acids causes the disease called
kwashiorkor.
Lecithin (present in eggs) and cephalins are phospholipids in which
two of the hydroxyl groups of glycerol are esterified with palmitic acid
whereas the third OH group in lecithin is esterified with chlone (CH ) N 3 3
+
N H 3 CH 2 CH 2 OH .
Adenosine (ribose + adenine) is a nucleoside while adenosine
monophosphate (AMP), adenosine diphosphate and adenosine
triphosphate (ATP) are all nucleotides.
Haemoglobin is a globular protein and the red colour of
haemoglobin is due to the iron protoporphyrin complex called the heme.
The bicarbonate/carbonic acid system i.e., HCO /H CO acts as the 3
–
2 3