BIOMOLECULES

By: Arun Goyal

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Previous Knowledge Testing:

You are familiar with the words, Carbohydrates, Proteins, Vitamins, DNA and RNA.

Q.1. What is the composition of Human body?

Q.2.What is role of carbohydrates in human body?

Q.3. How transference of genetic information take place from one generation to other?

Q.4. Why we prefer a balance diet?

Introduction
• A living system grows, sustains and reproduces itself. The most amazing thing
about a living system is that it is composed of non-living atoms and molecules

• The pursuit of knowledge of what goes on chemically within a living system falls
in the domain of biochemistry

• Living systems are made up of various complex biomolecules like carbohydrates,

proteins, nucleic acids, lipids, etc.

• Proteins and carbohydrates are essential constituents of our food. These

biomolecules interact with each other and constitute the molecular logic of life
processes

• In addition, some simple molecules like vitamins and mineral salts also play an
important role in the functions of organisms
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 Biomolecules
Biomolecules are the lifeless organic compounds which form the basis of life,
i.e., they build up the living system and responsible for their growth and
maintenance. E.g. Carbohydrates, proteins, vitamins, lipids etc.

The sequence that relates biomolecules to living organism is

Biomolecules →Cells → Tissues → Organs → Living organism

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Carbohydrates
Carbohydrates are produced by plants and form a very large group of naturally
occurring organic compounds.
 Examples: cane sugar, glucose, starch
 Most of them have a general formula, Cx(H2O)y, and were considered as
hydrates of carbon. (Old definition)
The molecular formula of glucose (C6H12O6) fits into this general formula,
C6(H2O)6.

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But all the compounds which fit into this formula may not be classified as
carbohydrates. Acetic acid (CH3COOH) fits into this general formula,
C2(H2O)2 but is not a carbohydrate.
Similarly, Rhamnose, C6H12O5 is a carbohydrate but does not fit in this
definition.

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Modern Definition of Carbohydrates:

Optically active polyhydroxy aldehydes or ketones or the compounds which produce

such units on hydrolysis.
Carbohydrates are also called saccharides

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I. Classification of Carbohydrates
(on the basis of their behaviour on hydrolysis)

1. Monosaccharides
2. Oligosaccharides
3. Polysaccharides

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1. Monosaccharide
Carbohydrate that cannot be hydrolysed further to give simpler unit of poly
hydroxy aldehyde or ketone is called a monosaccharide.
About 20 monosaccharides are known to occur in nature. Some common
examples are glucose, fructose, ribose, etc.

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2. Oligosaccharides
Carbohydrates that yield two to ten monosaccharide units, on
hydrolysis, are called oligosaccharides.
They are further classified as disaccharides, trisaccharides, tetra
saccharides, etc., depending upon the number of monosaccharides,
they provide on hydrolysis.
Disaccharides are most common. The two monosaccharide units
obtained on hydrolysis of a disaccharide may be same or different.

1. Sucrose + water  glucose and fructose

2. Maltose + water  two glucose molecules only.

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3. Polysaccharides
Carbohydrates which yield a large number of monosaccharide units
on hydrolysis are called polysaccharides.

 Examples: starch, cellulose, glycogen, gums, etc.

Starch + n water  n (Glucose)

Polysaccharides are not sweet in taste, hence they are also called non-
sugars. They are amorphous and insoluble in water.

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In Nut Shell:

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 Classification of Carbohydrates on the basis of Nature :
Reducing Sugars Non Reducing Sugars

All those carbohydrates which reduce Fehling’s All those carbohydrates which cannot reduce
solution and Tollens’ reagent are referred to Fehling’s solution and Tollens’ reagent are
as reducing sugars. All monosaccharides referred to as reducing sugars.
whether aldose or ketose are reducing sugars

e.g. Glucose or Fructose e.g. Sucrose

Free Aldehydic or Ketonic group is present Free Aldehydic or Ketonic group is not present

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Classification of Monosaccharides
(Based on number of carbon atoms and functional group)
 If a monosaccharide contains an aldehyde group, it is known as an aldose and
 a keto group, it is known as a ketose.

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 Glucose: Preparation and Structure

Glucose is colourless crystalline solid

Soluble in water

Sweet in taste
Preparation of Glucose
Glucose occurs freely in nature as well as in the combined form. It is
present in sweet fruits and honey. Ripe grapes also contain glucose in
large amounts.

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Structure of Glucose
 Glucose is an aldohexose and is also
known as dextrose.

It is the monomer of many of the larger

carbohydrates, namely starch, cellulose.

 It is probably the most abundant organic

compound on earth.
It belongs to D-series and is
a dextrorotatory compound.

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Structure of glucose based on below evidences
1. Its molecular formula was found to be C6H12O6
2. On prolonged heating with HI, it forms n-hexane, suggesting that all the six
carbon atoms are linked in a straight chain.

3. Glucose reacts with hydroxylamine to form an oxime and adds a molecule of

hydrogen cyanide to give cyanohydrin. These reactions confirm the presence of
a carbonyl group (>C = 0) in glucose

oxime
cyanohydrin
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5. Glucose gets oxidised to six carbon carboxylic acid (gluconic acid) on reaction
with a mild oxidising agent like bromine water. This indicates that the carbonyl
group is present as an aldehydic group.

6. On oxidation with nitric acid, glucose as well as gluconic acid both yield a
dicarboxylic acid, saccharic acid. This indicates the presence of a primary
alcoholic (–OH) group in glucose.

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Summary

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D and L notations (It’s base Glyceraldehyde structure)

 Glyceraldehyde contains one asymmetric carbon atom.

 Exists in two enantiomeric forms.

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Cyclic Structure of Glucose
 Glucose is found to exist in two different crystalline forms which are named as α
and β.
The α-form of glucose (m.p. 419 K) is obtained by crystallisation from
concentrated solution of glucose at 303 K
 while the β-form (m.p. 423 K) is obtained by crystallisation from hot and
saturated aqueous solution at 371 K

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 This behaviour could not be explained by the open chain structure for glucose.
It was proposed that one of the —OH groups may add to the —CHO group and
form a cyclic hemiacetal structure. It was found that glucose forms a six-
membered ring in which —OH at C-5 is involved in ring formation. This explains
the absence of —CHO group and also existence of glucose in two forms as shown
below

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Mutarotation
Mutarotation is the change in the optical rotation because of the change in the
equilibrium between two anomers, when the corresponding stereocenters
interconvert. Cyclic sugars show mutarotation as α and β anomeric forms
interconvert.

=+112o =+52.7o =+19o

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Anomeric carbon and anomers
The two cyclic hemiacetal forms of glucose differ only in the configuration of the
hydroxyl group at C1, called anomeric carbon (the aldehyde carbon before
cyclisation). Such isomers, i.e., α-form and β-form, are called anomers.
 The six membered cyclic structure of glucose is called pyranose
structure
(α or β), in analogy with pyran.
Pyran is a cyclic organic compound with one oxygen atom and five carbon
atoms in the ring. The cyclic structure of glucose is more correctly
represented by Haworth structure as given below.
Haworth structure

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Structure of Fructose (C6H12O6)
2 Keto-FG

Fructose exists in two cyclic forms (Anomers)

It belongs to D-series and is a

laevorotatory compound.

Seen in
Glucose
Haworth structures

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Disaccharides
Glycosidic linkage:
The two monosaccharides are joined together by an oxide linkage formed by the
loss of a water molecule. Such a linkage between two monosaccharide units
through oxygen atom is called glycosidic linkage.
Eg. Two monosaccharides are held together by a glycosidic linkage
between C1 of α-glucose and C4 α-glucose.

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Disaccharides
Glycosidic linkage:
The two monosaccharides are joined together by an oxide linkage formed by the
loss of a water molecule. Such a linkage between two monosaccharide units
through oxygen atom is called glycosidic linkage.
(i) Sucrose: One of the common disaccharides is sucrose which on hydrolysis
gives equimolar mixture of D-(+)-glucose and D-(-) fructose.

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These two monosaccharides are held together by a glycosidic linkage
between C1 of α-glucose and C2 of β-fructose.
Since the reducing groups of glucose and fructose are involved in glycosidic
bond formation, sucrose is a non reducing sugar.
NO Free
anomeric C,
Non-
reducing
sugar

 Sucrose is dextrorotatory but after hydrolysis gives dextrorotatory glucose and

laevorotatory fructose. Since the laevorotation of fructose (–92.4°) is more than
dextrorotation of glucose (+ 52.5°), the mixture is laevorotatory.
 Thus, hydrolysis of sucrose brings about a change in the sign of rotation, from dextro (+) to
laevo (–) and the product is named as invert sugar
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(ii) Maltose: It’s a disaccharide, maltose is composed of two α-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 C1 of second glucose in solution and it
shows reducing properties so it is a reducing sugar.
Free anomeric
C, Reducing
sugar

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(iii) Lactose: (milk sugar since this disaccharide is found in milk)
 It is composed of β-D-galactose and β-D-glucose.
 The linkage is between C1 of galactose and C4 of glucose.
 Hence it is also a reducing sugar.
Free anomeric C,
Reducing sugar

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Polysaccharides
 Polysaccharides contain a large number of monosaccharide
units joined together by glycosidic linkages.
Polysaccharides are the most commonly encountered
carbohydrates in nature. They mainly act as the food storage
or structural materials.

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I. Starch:
1. Starch is the main storage polysaccharide of plants.
2. It is the most important dietary source for human beings. High content of starch
is found in cereals, roots, tubers and some vegetables.
3. It is a polymer of α-glucose, consists of two components

1. Amylose
2. Amylopectin

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1. Amylose

i. It’s water soluble component which constitutes about 15-20%

of starch.

ii. Chemically amylose is a long unbranched chain with 200-1000

α-D-(+)-glucose units held by C1– C4 glycosidic linkage.

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2. Amylopectin
i. It’s insoluble in water and constitutes about 80-85% of starch.
ii. It is a branched chain polymer of α-D-glucose units in which chain is formed
by C1–C4 glycosidic linkage whereas branching occurs by C1–C6 glycosidic
linkage

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Starch

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II. Cellulose
1. Cellulose occurs exclusively in plants and it is the most abundant organic
substance in plant kingdom.
2. It’s a predominant constituent of cell wall of plant cells.
3. Cellulose is a straight chain polysaccharide composed only of β-D-glucose
units which are joined by glycosidic linkage between C1 of one glucose unit
and C4 of the next glucose unit.
C1

C4

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III Glycogen:

1. The carbohydrates are stored in animal body as glycogen.

2. It is also known as animal starch because its structure is

Compone
similar to amylopectin and is rather more highly branched.
nt of
starch

3. It is present in liver, muscles and brain. amylopectin

4. When the body needs glucose, enzymes break the glycogen

down to glucose.

5. Glycogen is also found in yeast and fungi.

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polysaccharides

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Summary

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Importance of Carbohydrates
1. Carbohydrates are essential for life in both plants and animals. They form a major
portion of our food.
2. Honey has been used for a long time as an instant source of energy by ‘Vaids’in
ayurvedic system of medicine.
3. Carbohydrates are used as storage molecules as starch in plants and glycogen in
animals. Cell wall of bacteria and plants is made up of cellulose.
4. We build furniture, etc. from cellulose in the form of wood and clothe ourselves
with cellulose in the form of cotton fibre.
5. They provide raw materials for many important industries like textiles, paper,
lacquers and breweries.
6. Two aldopentoses namely, D-ribose and 2-deoxy-D-ribose are present in nucleic
acids.
7. Carbohydrates are found in bio-system in combination with many proteins and
lipids.

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Proteins
1. Proteins are the most abundant biomolecules of
the living system.
2. Chief sources of proteins are milk, cheese,
pulses, peanuts, fish, meat, etc.
3. They occur in every part of the body and form
the fundamental basis of structure and functions
of life.
4. They are also required for growth and
maintenance of body. The word protein is
derived from Greek word, “proteios” which
means primary or of prime importance.
5. All proteins are polymers of α-amino acids.
Protein rich Food
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Amino Acids
1. Amino acids contain amino (–NH2) and carboxyl (–COOH)
functional groups.
2. Depending upon the relative position of amino group with
respect to carboxyl group, the amino acids can be classified
as α, β, γ, δ and so on. Only α-amino acids are obtained on
hydrolysis of proteins.
3. They may contain other functional groups also.
4. All α-amino acids have trivial names, which usually reflect
the property of that compound or its source.
5. Glycine is so named since it has sweet taste (in Greek Glycine
glykos means sweet) and tyrosine was first obtained from
cheese (in Greek, tyros means cheese.)
6. Amino acids are generally represented by a three letter
symbol, sometimes one letter symbol is also used.
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 Acdi Acdi
c c

Basic Basic
Basi
c

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Classification of Amino Acids
Acidic, basic or neutral depending upon the relative number of amino and
carboxyl groups in their molecule.
Equal number of amino and carboxyl groups makes it neutral; more number of
amino than carboxyl groups makes it basic and more carboxyl groups as compared
to amino groups makes it acidic.

Acidic Amino Acids Aspartic acid

Glutamic Acid
Basic Amino Acids Lysine
Arginine
Acidic (Pka=3.9) Histidine

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Classification of Amino Acids
 The amino acids, which can be synthesised in the body, are known as
Nonessential amino acids. (11)
On the other hand, those which cannot be synthesised in the body and must
be obtained through diet, are known as Essential amino acids.(9)

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 Amino acids are usually colourless, crystalline solids.
Amino acids 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.
aqueous

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 No asymmetric carbon
Except glycine, all other naturally occurring
α-amino acids are optically active,
since the α-carbon atom is asymmetric. Optically
inactive

 These exist both in ‘D’ and ‘L’forms.

Most naturally occurring amino acids have L-

configuration. L-Amino acids are represented
by writing the –NH2 group on left hand side. L

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Structure of Proteins
 Proteins are the polymers of α-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.

glycine alanine

when carboxyl group of

glycine combines with
dipeptide the amino group of
alanine we get a
dipeptide, glycylalanine.
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If a third amino acid combines to a dipeptide, the product is called a
tripeptide. A tripeptide contains three amino acids linked by two
peptide linkages.
Similarly when four, five or six amino acids are linked, the respective
products are known as tetrapeptide, pentapeptide or hexapeptide,
respectively.
When the number of such amino acids is more than ten, then the
products are called polypeptides. A polypeptide with more thanhundred
amino acid residues, having molecular mass higher than 10,000 u is
called a protein.
 Polypeptides with fewer amino acids are likely to be called proteins
if they ordinarily have a well defined conformation of a protein.
Example: Insulin which contains 51 amino acids, It’s a protein.

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Classification of Proteins
(Based on the basis of their molecular shape)

(a) Fibrous proteins (b) Globular proteins

1. When the polypeptide chains 1. This structure results when
run parallel and are held together the chains of
by hydrogen and disulfide bonds, polypeptides coil around to
then the fiber-like structure is give a spherical shape.
formed. 2. These are usually soluble in
2. These proteins are generally Water.
insoluble in water. These are
water-insoluble proteins.
Example: keratin (present in hair, Example: Insulin and albumins
wool, and silk) are common examples of
myosin (present in muscles), etc. globular proteins
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Difference between Fibrous and Globular Proteins

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 Structure and shape of proteins
primary, secondary, tertiary and quaternary, each level
being more complex than the previous one.
1. Primary structure of proteins:
i. Proteins may have one 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.
ii. Any change in this primary structure i.e.,
the sequence of amino acids creates a
different protein.

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2. Secondary structure of proteins:
i.The secondary structure of protein refers to the shape in which a long
polypeptide chain can exist.

ii. They are found to exist in two different types of structures

iii. α-helix and β-pleated sheet structure.

iii. These structures arise due to the regular folding of the backbone of the
polypeptide chain due to hydrogen bonding between -C=O and –NH–
groups of the peptide bond.

iv. α-Helix is one of the most common ways in which a polypeptide chain
forms all possible hydrogen bonds by twisting into a right handed
screw (helix) with the –NH group of each amino acid residue hydrogen
bonded to the C=O of an adjacent turn of the helix.

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In β-structure all peptide chains are stretched out to nearly maximum
extension and then laid side by side which are held together by
intermolecular hydrogen bonds.
The structure resembles the pleated folds of drapery and therefore is known
as β-pleated sheet.

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3. Tertiary structure of proteins:

i. The tertiary structure of proteins

represents overall folding of the
polypeptide chains i.e., further
folding of the secondary structure.

ii. It gives rise to two major molecular

shapes. Namely, fibrous and globular.
The main forces which stabilise the
2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages,
van der Waals and electrostatic forces
of attraction.

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4. Quaternary structure of proteins:

i. Some of the proteins are composed of two

or more polypeptide chains referred to as
sub-units.

ii. The spatial arrangement of these subunits

with respect to each other is known as
quaternary structure.

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Denaturation of Proteins
Native Protein:
Protein found in a biological system with a unique three-
dimensional structure and biological activity is called a native
protein.
Denaturation:
i. When a protein in its native form, is subjected to 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.
ii. During denaturation 2° and 3° structures are destroyed but
1º structure remains intact.
i. Examples:
The coagulation of egg white on boiling.
curdling of milk which is caused due to the formation of lactic
acid by the bacteria present in milk.
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Enzymes
(Biocatalysts works under mild conditions in living organisms)

Enzymes are biological molecules (typically proteins) that

significantly speed up the rate of the chemical reactions that
take place within cells.
They are vital for life and serve a wide range of important
functions in the body, such as aiding in digestion
and metabolism.
 Almost all the enzymes are globular proteins.
Enzymes are very specific for a particular reaction and for a
particular substrate.
They are generally named after the compound or class of
compounds upon which they work.

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 Example: Hydrolysis of Maltose by Maltase enzyme

Example: Oxidoreductase

 The enzymes which catalyse the oxidation

of one substrate with simultaneous
reduction of another substrate are named
as oxidoreductase enzymes

Note: The ending of the name of an enzyme is -ase

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Mechanism of Enzyme Action
1. There is a lock and key
arrangement between the an
enzyme and a substrate.
2. Substrates bind at active site,
temporarily forming an
enzyme-substrate (E-S)
complex.
3. The E-S complex undergoes
internal rearrangements that
form the product.
4. The enzyme gets regenerated
for the next molecule of the
substrate.

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VITAMINS
 Vitamines are complex organic molecules which cannot be
produced by the body and must be supplied in small amounts
in diet to carry out essential metabolic reactions which are
required for normal growth and maintenance of the body.

Classification :
Water soluble vitamins : Soluble in Fat soluble vitamins :
water. Must be supplied regularly in diet Soluble in fat and oils. Stored in
as they are regularly excreted in urine liver and adipose tissues e.g.,
(except vitamin B12) Vitamin- A, D, E and K
Vitamin- B1, B2, B6, B12 and C

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Name of Vitamin Important Sources Deficiency Diseases

Fish liver oil, Milk, butter, Night blindness,

Vitamin A egg yolk, green and yellow Xerophthalmia (hardening of
vegetables. cornea of eye).
Yeast, milk, green vegetables, Beriberi (loss of appetite,
Vitamin B1
cereals, fruits, egg yolk. retarded growth)

Cracked lips, sore tongue,

Egg yolk, liver, milk, green
Vitamin B2 digestive disorders and burning
leafy vegetables.
sensation of the skin.

Milk, egg yolk, cereals, yeast, Nervous disturbances and

Vitamin B6
legumes. convulsions.
Pernicious anaemia (RBC
Vitamin B12 Meat, fish, kidney, eggs.
deficient in haemoglobin)

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 Citrus fruits, amla and green
Vitamin C Scurvy (bleeding gums)
leafy vegetables.
Rickets (bone deformities in
Exposure to sunlight, fish children) and osteomalacia
Vitamin D
and egg yolk (soft bones and joint pain in
adults)
Milk, ghee, vegetable oils
like wheat germ oil, Increased fragility of RBCs
Vitamin E
sunflower oil, cotton seed and muscular weakness
oil.

Vitamin H Milk, yeast, liver, kidney. Loss of hair, dermatitis.

Green leafy vegetables, fish,

Vitamin K Increased blood clotting time
meat, cereals.

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Structure of Nucleic Acids

 Nucleic acids are the polymers of nucleotides

present in nucleus of all living cells and play an
important role in transmission of the hereditary
characteristics and biosynthesis of proteins

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 Nitrogenous
bases

Nitrogenous bases or often simply bases, are

nitrogen-
containing biological compounds that form
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nucleosides.
 nucleoside

Nucleoside:
A unit formed by the attachment of a base to 1'
position of sugar is known as nucleoside.

nucleotide

Nucleotide:
When nucleoside is linked to phosphoric acid at 5′-position
of sugar moiety, we get a nucleotide.

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Amount of purine bases is
always equal to that of
pyrimidine bases. Purine base
of one strand of DNA
molecule pairs with pyrimidine
base of the other strand.
Adenine (A) pairs with thymine
(T)through two H-bonds
(A=T) and guanine (G) pairs
with cytosine (C) through three
H-bonds (G=C).
In case of RNA, adenine (A)
pairs with uracil
(U), (A U).

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DOUBLE AND SINGLE STRAND STRUCTURE
 Thanks
Referenc
e
NCERT Text Book Class XII
Images are taken from different websites and open sources available in google images.
Chemistry Reference books

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