Biomolecules

Part-01

Biomolecules are chemical compounds which are building blocks of life and perform important functions in
living organisms. The general biomolecules that our food contains are :

Biomolecules
• Carbohydrates
• Proteins
• Enzymes
• Vitamins
• Nucleic acids
• Hormones

1. Carbohydrate
Thus, General formula of carbohydrate can be written as Cx (H2O)y
Here, x=y or x≠y
Hence these are called, Hydrates of carbon
Exceptions
• Rhamnose (C6H12O5) is a carbohydrate, but it does not fit in this formula.
• Acetic acid (CH3COOH) is not a carbohydrate, but it fit in this formula.

Simplest ratio ⎯⎯→ C : H : O

1:2 :1

1. Glucose ⎯→ Mol. Formula (C6H12O6)

Glucose ⎯→ C6 (H2O)6
2. Sucrose ⎯→ Mol. Formula (C12H22O11)
Sucrose ⎯→ C12 (H2O)11

New definition of carbohydrates

Optically active polyhydroxy aldehydes and polyhydroxy ketones or compounds which give such compounds
on hydrolysis are called carbohydrates.
Only dihydroxy acetone is optically inactive carbohydrate.

Carbo hydrates are also called saccharides (greek word: saccharon means sugar).
 Classification of Saccharides on the basis of behaviour on hydrolysis
• Monosaccharides
• Oligosaccharides
• Polysaccharides

Monosaccharides
• A carbohydrate that cannot be hydrolysed further to give simpler unit of polyhydroxy aldehyde or ketone is
called a monosaccharide.
• About 20 monosaccharides are known to occur in nature.
Example: glucose, fructose, ribose, etc.

Monosaccharides are further classified on the basis of number of carbon atoms and the functional group present
in them. If a monosaccharide contains an aldehyde group, it is known as an aldose and if it contains a keto
group, it is known as a ketose. Number of carbon atoms constituting the monosaccharide is also introduced in
the name as is evident from the examples given in table.

No. of Carbon Aldose Ketose

Atoms (these contain aldehyde functional group) (these contain ketone functional group)
3 Aldotriose = Glyceraldehyde Ketotriose = Dihydroxy ketone
4 Aldotetrose = Erythrose Ketotetrose = Erythrulose
5 Aldopentose = Ribose Ketopentose = Ribulose
6 Aldohexose = Glucose Ketohexose = Fructose
7 Aldoheptose = manohaptose Ketoheptose = sedoheptulose

Oligosaccharides
• Carbohydrates that yield two to ten monosaccharide units, on hydrolysis, are called oligosaccharides.
• They are further classified as disaccharides, trisaccharides, tetrasaccharides etc. depending upon the number of
monosaccharides which provide on hydrolysis.
Example: sucrose( glucose + fructose) , maltose( glucose + glucose) etc.

Polysaccharides
Carbohydrates which yield a large number of monosaccharide units on hydrolysis are called polysaccharides.
Some common examples are starch, cellulose, glycogen, etc. Polysaccharides are not sweet in taste, hence they
are also called non-sugars.

The carbohydrates may also be classified as either reducing or non-reducing sugars.

Reducing sugars
1. They reduce Fehling solution and Tollen’s reagent
2. All monosaccharides and disaccharides in which aldehydic and ketonic groups are free, behave as reducing
sugars.
Example : Glucose, Fructose, Maltose and lactose.
 Non-reducing sugars
1. They do not reduce Fehling’s solution and Tollen’s reagent.
2. All polysaccharides and disaccharides in which aldehydic or ketonic groups are bonded behave as
non-reducing sugars.
Example : Sucrose, Starch, Glycogen

Monosaccharides
Glucose
1. Laboratory Method
From Sucrose (Cane sugar)

On hydrolysis of sucrose, the sign of rotation changes from dextro (+) to laevo (–), so sucrose is called invert
sugar.

Separation of glucose from fructose

• While cooling, alcohol is added to the reaction mixture
• Glucose crystals are removed by cooling
• Glucose being insoluble in alcohol crystallizes out first
• Crystals of glucose are separated by filtration
• Fructose being more soluble in alcohol, remains in the solution

2. Commercial Method
From Starch

Purification of glucose
• The coloured impurities are removed by adding activated charcoal
• Glucose crystals are removed by cooling

Chemical reactions of Glucose

(a) Reaction with NH2OH
(b) Reaction with HCN

(c) Oxidation
Oxidation of glucose to six carbon carboxylic acid (gluconic acid) indicates that the carbonyl group is present as
an aldehydic group.

(i) Oxidation with Br2 water

(ii) Oxidation by Tollen’s Reagent, Fehling solution and Benedict’s solution

Oxidation of glucose to six carbon containing di carboxylic acid indicates the presence of primary Alcohol group.

(iii) Oxidation by conc. HNO3

(d) Acetylation of glucose with acetic anhydride gives glucose penta acetate which confirms the presence of
five –OH groups.

(e) Reaction with Phenyl Hydrazine (Osazone formation):

When carbohydrates react with excess of phenyl hydrazine then osazone is formed
 Biomolecules
Part-02

Open chain structure of Glucose

The exact spatial arrangement of different –OH groups was given by Fischer after studying many other
properties.
Glucose is correctly named as D(+)-glucose. The meaning of D– and L– notations is given as follows.

D before the name of glucose represents the configuration whereas (+) represents dextrorotatory nature of the
molecule.

Epimers : Optically active diastereomers which have different configuration about one of the chiral carbon and
same configuration at remaining carbon are called epimers.

These have different configuration only at second carbon so called as C-2 epimers.
Cyclic Structure of Glucose
1. Glucose does not give 2,4-DNP test and Schiff’s test.
2. Glucose does not form addition product with NaHSO3.
3. Penta acetate of glucose does not react with NH2OH

D-Glucose is found to exist in two different crystalline forms which are named as  and .
-form: M.P. = 419 K
Obtained by crystallization of concentrated solution of glucose at 303K
-form: M.P. = 423 K
Obtained by crystallization of concentrated solution of glucose at 371K

It was proposed that one of the –OH groups may add to the –CHO group and form a cyclic hemiacetal structure.

The six membered cyclic structure of glucose is called pyranose structure in analogy with Pyran.

Cyclic epimers are called anomers, so -D-Glucose and -D-Glucose are also called anomers which have first
carbon as anomeric (hemiacetal) Carbon.

Mutarotation : -form and -form of D-Glucose slowly change optical rotation in aqueous solution to yield the
same final rotation (=+52.7°), this process is known as Mutarotation. It becomes possible due to
tautomerisation from cyclic hemiacetal form to acyclic form.
Fructose
Fructose is called fruit sugar
Fructose is an important ketohexose. It is obtained along with glucose by the hydrolysis of sucrose.
Molecular formula of fructose is also C6H12O6 and it belongs to D-series. It is laevorotatory compound

It also exists in two cyclic forms which are obtained by the addition of –OH at C5 to the group.

These differ at C2 -Carbon so called C-2 epimers.

Cyclic structures of Fructose are also called fructofuranose structure due to analogy with furan.
Disaccharides

(i) Sucrose : One of the common disaccharides is sucrose which on hydrolysis gives equimolar mixture of D- (+)-
glucose and D-(-) fructose.

These two monosaccharides are held together by a glycosidic linkage between C 1 of -glucose and C2 of
-fructose. Since the reducing groups of glucose and fructose are involved in glycosidic bond formation,
sucrose is a non reducing sugar.

Hydrolysis of sucrose brings about a change in the sign of rotation, from dextro (+) to laevo (–) and the product
is named as invert sugar.

(ii) Maltose: Another disaccharide, maltose is composed of two a-D-glucose units in which C1 of one glucose (I) is
linked to C4 of another glucose unit (II). The free aldehyde group can be produced at C 1 of second glucose in
solution and it shows reducing properties so it is a reducing sugar.
(iii) Lactose : It is more commonly known as milk sugar since this disaccharide is found in milk. It is composed of
-D-galactose and -D-glucose. The linkage is between C1 of galactose and C4 of glucose. It is also a reducing
sugar.

Polysaccharides

(i) Starch: Starch is the main storage polysaccharide of plants. It is the most important dietary source for human
beings. High content of starch is found in cereals, roots, tubers and some vegetables. It is a polymer of -glucose
and consists of two components—

Amylose and Amylopectin :

Amylose is hot water soluble component which constitutes about 15-20% of starch. Chemically amylose is a
long unbranched chain with 200-1000 -D-(+)-glucose units held by C1– C4 glycosidic linkage.

Amylopectin is insoluble in hot water and constitutes about 80-85% of starch. It is a branched chain polymer of
-D-glucose units in which chain is formed by C1–C4 glycosidic linkage whereas branching occurs by C1–C6
glycosidic linkage.
(ii) Glycogen : The carbohydrates are stored in animal body as glycogen. It is also known as animal starch because
its structure is similar to amylopectin and is rather more highly branched. It is present in liver, muscles and brain.
When the body needs glucose, enzymes break the glycogen down to glucose. Glycogen is also found in yeast
and fungi.

(iii) Cellulose : Cellulose occurs exclusively in plants and it is the most abundant organic substance in plant kingdom.
It is a predominant constituent of cell wall of plant cells. Cellulose is a straight chain polysaccharide composed
only of -D-glucose units which are joined by glycosidic linkage between C1 of one glucose unit and C4 of the
next glucose unit.
 Biomolecules
Part-03

Proteins
The word protein is derived from Greek word, “proteios” which means primary or of prime importance.
All proteins are polymers of -L-amino acids.

Amino acids: Amino acids contain amino (–NH2) and carboxyl (–COOH) functional groups. Depending upon
the relative position of amino group with respect to carboxyl group, the amino acids can be classified as , , ,
 and so on. Only -amino acids are obtained on hydrolysis of proteins. They may contain other functional
groups also.

Classification of -Amino acids

1. Acidic amino acids
2. Basic amino acids
3. Neutral amino acids

1. Acidic amino acids:- Number of acidic group > Number of basic groups
1. Aspartic acid [Asp] :-

2. Glutamic acid [Glu] :-

2. Basic amino acids:- Number of basic groups > Number of acidic groups
1. Arginine [Arg] :-

2. Lysine [Lys] :-

3. Histidine [His] :-
3. Neutral amino acids:- Number of acidic groups = Number of basic groups

1. Glycine [Gly] :- 2. Alanine [Ala] :-

3. Proline [Pro] :- 4. Valine [Val] :-

5. Leucine [Leu] :- 6. Phenyl alanine [Phe] :-

7. Isoleucine [Ile] :- 8. Cysteine [Cys] :-

9. Methionine [Met] :- 10. Asparagine [Asn] :-

11. Glutamine [Gln] :- 12. Tryptophan [Trp] :-

13. Serine [Ser] :- 14. Threonine [Thr] :-

15. Tyrosine [Tyr] :-

Classification of Amino Acids :

Amino acids are classified as acidic, basic or neutral depending upon the relative number of amino and carboxyl
groups in their molecule.
The amino acids, which can be synthesised in the body, are known as non-essential amino acids. On the other
hand, those which cannot be synthesised in the body and must be obtained through diet, are known as essential
amino acids.
 Amino acids are usually colourless, crystalline solids. These are water-soluble, high melting solids and behave
like salts rather than simple amines or carboxylic acids. This behaviour is due to the presence of both acidic
(carboxyl group) and basic (amino group) groups in the same molecule.

In aqueous solution, the carboxyl group can lose a proton and amino group can accept a proton, giving rise to
a dipolar ion known as zwitter ion. This is neutral but contains both positive and negative charges.

In zwitter ionic form, amino acids show amphoteric behaviour as they react both with acids and bases.

Except glycine, all other naturally occurring -amino acids are optically active, since the -carbon atom is
asymmetric. These exist both in ‘D’ and ‘L’ forms. Most naturally occurring amino acids have L-configuration.
L-Aminoacids are represented by writing the –NH2 group on left hand side.

Structure of Proteins :
Proteins are the polymers of -amino acids and they are connected to each other by peptide bond or peptide
linkage. Chemically, peptide linkage is an amide formed between –COOH group and –NH2 group.

The reaction between two molecules of similar or different amino acids, proceeds through the combination of
the amino group of one molecule with the carboxyl group of the other. This results in the elimination of a water
molecule and formation of a peptide bond –CO–NH–.

Proteins can be classified into two types on the basis of their molecular shape.
(a) Fibrous proteins
When the polypeptide chains run parallel and are held together by hydrogen and disulphide bonds, then fibre-
like structure is formed. Such proteins are generally insoluble in water. Some common examples are keratin
(present in hair, wool, silk) and myosin (present in muscles), etc.
(b) Globular proteins
This structure results when the chains of polypeptides coil around to give a spherical shape. These are usually
soluble in water. Insulin and albumins are the common examples of globular proteins.
Structure and shape of proteins can be studied at four different levels, i.e., primary, secondary, tertiary and
quaternary, each level being more complex than the previous one.
 O
C
C
O
H O
H
O
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C
H C N
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H
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H N
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1. Primary structure of Proteins:

The primary structure of proteins refers to the sequence of amino acids held together by peptide bonds.
Any change in this sequence of amino acids creates a different protein.

2. Secondry structure of Proteins:

 (i) 𝜶-Helix structure :- In 𝛼-helix a polypeptide chain forms all possible hydrogen bonds by twisting into right-
handed screw

(ii) 𝛃 - pleated sheet structure :- In 𝛽- structure all peptide chains are stretched out to nearly maximum
extension and then laid side by side which are held together by inter molecular hydrogen bonds.

3. Tertiary structure of Proteins:

The tertiary structure of proteins represents overall folding of the peptide chains. It gives rise to two molecular
shapes fibrous and globular.
4. Quaternary structure of Proteins:
Some of the proteins are composed of two or more polypeptide chains referred to as sub-units. The special
arrangement of these subunits with respect to each other is known as quaternary structure.

Denaturation of Proteins :
Physical change like change in temperature or chemical change like change in pH, the hydrogen bonds are
disturbed. Due to this, globules unfold and helix get uncoiled and protein loses its biological activity. This is
called denaturation of protein.
The coagulation of egg white on boiling is a common example of denaturation. Another example is curdling of
milk which is caused due to the formation of lactic acid by the bacteria present in milk.
During denaturation secondary and tertiary structures are destroyed but primary structure remains unchanged.
 Biomolecules
Part-04

Enzymes
• Enzymes are biological catalysts which bring about chemical reactions in living cells. They are produced by the
living organism and are usually present in only very small amounts in the various cells.
• Enzymes are very specific for a particular reaction and for a particular substrate.
• All enzymes are globular proteins.
Examples: Pepsin, Trypsin, Proteases etc.

Vitamins
The 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 are called vitamins.

1. Fat soluble vitamins : A, D, E and K

2. Water soluble vitamins : B and C

S.N. Vitamin Chemical name Deficiency disease Source

1 Vitamin-A Retinol Xerophthalmia (Hardening of Fish liver oil, Carrot,
cornea of eye) and Night Butter, Milk
blindness
2 Vitamin-B1 Thiamine Beri-beri (Loss of appetite and Yeast, Milk, Green
retarded growth), Paralysis vegetables, Cereals
3 Vitamin-B2 Riboflavin Cheilosis (Fissuring at corners Milk, Egg white, Liver,
of mouth and lips) Kidney
4 Vitamin-B6 Pyridoxine Convulsion Milk, Yeast, Egg yolk,
Cereals
5 Vitamin-B12 Cyanocobalamine Pernicious anaemia (RBC Fish, Meat, Egg, curd
deficient in Hb)
6 Vitamin-C Ascorbic acid Scurvy (bleeding gums) Citrus fruits, Amla
Green leafy vegetables
7 Vitamin-D Calciferol Rickets (Bone deformities in Exposure to sunlight,
children) Fish, Egg yolk
Osteomalacia (soft bones &
joint pain in adults)
8 Vitamin-E Tocoferol Increased fragility of RBC Vegetable oil, Sunflower
Muscular weakness oil
9 Vitamin-K Phylloquinone Increased blood clotting time Green leafy vegetables
Nucleic acids
It has been observed that nucleus of a living cell is responsible for the transmission of inherent characters, also
called heredity. The particles in nucleus of the cell, responsible for heredity, are called chromosomes which are
made up of proteins and another type of biomolecules called nucleic acids.
These are mainly of two types, the deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). Since nucleic acids
are long chain polymers of nucleotides, so they are also called polynucleotides.

1. Chemical composition of Nucleic Acids :

Complete hydrolysis of DNA (or RNA) yields a pentose sugar, phosphoric acid and nitrogen containing
heterocyclic compounds (called bases). In DNA molecules, the sugar moiety is -D-2-deoxyribose whereas in
RNA molecule, it is -D-ribose.

DNA contains four bases viz. adenine (A), guanine (G), cytosine (C) and thymine (T). RNA also contains four
bases, the first three bases are same as in DNA but the fourth one is uracil (U).
2. Structure of Nucleic Acids :-
A unit formed by the attachment of a base to 1' position of sugar is known as nucleoside. In nucleosides, the
sugar carbons are numbered as 1', 2', 3', etc. in order to distinguish these from the bases. When nucleoside is
linked to phosphoric acid at 5'-position of sugar moiety, we get a nucleotide.

Nucleotides are joined together by phosphodiester linkage between 5' and 3' carbon atoms of the pentose
sugar. A simplified version of nucleic acid chain is as shown below. Fig.

Information regarding the sequence of nucleotides in the chain of a nucleic acid is

called its primary structure. Nucleic acids have a secondary structure also.

James Watson and Francis Crick gave a double strand helix structure for DNA
(Fig.). Two nucleic acid chains are wound about each other and held together by
hydrogen bonds between pairs of bases. The two strands are complementary to
each other because the hydrogen bonds are formed between specific pairs of
bases.

Adenine forms hydrogen bonds with thymine whereas cytosine forms hydrogen
bonds with guanine.
In secondary structure of RNA, helix are present which are only single stranded.
Sometimes they fold back on themselves to form a double helix structure.

RNA molecules are of three types and they perform different functions.
1. messenger RNA (m-RNA)
2. ribosomal RNA (r-RNA)
3. transfer RNA (t-RNA).
Hormones
Hormones are biomolecules which are produced in the ductless (endocrine) glands and are carried to different
parts of the body by the blood stream where they control various metabolic processes. These are required in
minute quantites and unlike fats and carbohydrates these are not stored in the body but are continuously
produced.
Some important hormones along with the sources and functions are summarised below :

Name Organ of secretion Functions

(I) Steroidal hormones
(A) Sex hormones
(a) Androgens (Testosterone) Testes Control the development and normal
functioning of Androsterone and male
sex organs.
(b) Estrogens (Estrone, Ovary Control the development and normal
Estradiol, Estriol) functioning of female sex organs.
(c) Gestogens (Progesterone) Corpus luteum Control the development and
maintenance of pregnancy.
(B) Adrenal cortex hormones or Adrenal cortex Regulate the metabolism of fats,
corticoids (Cortisone, proteins and carbohydrates; control the
Corticosterone balance of water and minerals in the
Aldosterone etc.) body.
(II) Peptide hormones
(i) Oxytocin Posterior pituitary gland Controls the contraction of the uterus
after child birth and releases milk from
the mammary glands.
(ii) Vasopressin Posterior pituitary gland Controls the reabsorption of water in
the kidney.
(iii) Angiotensin II Blood plasma of Potent vasoconstrictor i.e. contracts the
persons with high blood blood vessels.
pressure.
(iv) Insulin Pancreas Controls the metabolism of glucose,
maintains glucose level in the blood.
(III) Amine hormones
(i) Adrenaline or Epinephrine Adrenal medulla It is an amine compound and was the
first hormone to be isolated. Prepares
animals and humans for emergency in
many ways by raising the pulse rate,
blood pressure etc. stimulates the
breakdown of liver glycogen into blood
glucose and fats into fatty acids during
emergency. These properties make
adrenaline as one of the most valuable
drugs used in medicine.
(ii) Thryoxine Thyroid gland Controls metabolism of carbohydrates,
lipids and proteins.