Biomolecules

Carbohydrates – Definition, Classification (aldoses and ketoses), monosaccahrides (glucose

and fructose), D-L configuration- oligosaccharides (sucrose, lactose, maltose),
polysaccharides (starch, cellulose, glycogen); Importance of carbohydrates. Carbohydrates:
definition, classification - mono
(aldose, ketose), oligo (di, tri, tetra saccharides) and polysaccharides with examples: reducing
sugars and non-reducing sugars – examples and uses.
Establishment of structures for glucose and fructose (open and cyclic) heating with HI,
reaction with hydroxylamine, bromine water, acetic anhydride, nitric acid and phenyl
hydrazine. Test for glucose and fructose (bromine water test with equation). Disaccharides –
structures of sucrose, maltose
and lactose (glycosidic linkage). Polysaccharides – starch, cellulose, glycogen.
Proteins – structural units of proteins. Basic idea of - amino acids, peptide bond,
polypeptides, proteins, structure of proteins - primary, secondary, tertiary structure and
quaternary structures (qualitative idea only), denaturation of proteins. Enzymes, hormones -
elementary idea only.
Proteins: Amino acids – general structure, classification and zwitter ion formation.
Isoelectric point.
Classification of proteins on the basis of molecular shape; primary, secondary, tertiary and
quaternary, structures of proteins, denaturation of proteins. (Definitions only. Details and
diagrams are not required).
Vitamins - Classification and functions. Vitamins A, B, C, D, E and K: classification (fat
soluble and water soluble), deficiency diseases. (Chemical names and structures are not
required).
Nucleic Acids - DNA and RNA. Nucleic acids: basic unit – purine and pyrimidine, DNA –
structure (double helical), RNA (No chemical structure required). Differences between DNA
and RNA

Carbohydrates:The organic compounds that include polyhydroxy aldehydes and polyhydroxy

ketones .
Classification –(i) mono (aldose, ketose),
Mono sacccharides cannot be broken into simpler units on hydrolysis .eg. glucose and fructose .

(ii) oligo (di, tri, tetra saccharides)

Disacccharides – will produce two mono sacccharides on hydrolysis.Eg. sucrose, lactose and
maltose .
one molecule of sucrose on hydrolysis gives one molecule of glucose and one molecule of fructose
whereas maltose gives two molecules of only glucose.
Poly saccharides- will produce a large number of mono sacccharides on hydrolysis.eg. starch
cellulose and glycogen .

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Polysaccharides contain a large number of monosaccharide units joined together by glycosidic
linkages. These are the most commonly encountered carbohydrates in nature. They mainly act as
the food storage or structural materials.
(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 α-glucose and consists of two components—
Amylose and Amylopectin. Amylose is water soluble component which constitutes
about 15-20% of starch. Chemically amylose is a long unbranched chain with 200-1000
α-D-(+)-glucose units held together by C1– C4 glycosidic linkage. Amylopectin is
insoluble in water and constitutes about 80- 85% of starch. 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.
(ii) 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 β-D-glucose units which are joined by glycosidic linkage
between C1 of one glucose unit and C4 of the next glucose unit.
(iii) 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.
Reducing sugars.-Monosacccharides which reduce Fehling’s solution and Tollen’s reagent .
glucose and fructose .
Non reducing sugars – Disacccharides which does not reduce Fehling’s solution and Tollen’s
reagent .eg. sucrose .

Importance of carbohydrates.
Carbohydrates are essential for life in both plants and animals. They form a major portion of our
food. Honey has been used for a long time as an instant source of energy by ‘Vaids’ in ayurvedic
system of medicine. 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. We build furniture, etc. from
cellulose in the form of wood and clothe ourselves with cellulose in the form of cotton fibre. They
provide raw materials for many important industries like textiles, paper, lacquers .Two
aldopentoses viz. D-ribose and 2-deoxy-D-ribose are present in nucleic acids. Carbohydrates are
found in biosystem in combination with many proteins and lipids.
Qn.Sucrose is a non reducing sugar. Give reason .
Because in sucrose the reducing groups of glucose and fructose are not free. They are involved
in the formation of glycosidic linkage in sucrose .
Qn. Hydrolysis of sucrose is called inversion of sugar . Give reason .
Sucrose is dextro rotatory, but on hydrolysis it gives an equimolar mixture of glucose and fructose
which is leavorotatory .

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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.
Establishment of structures for glucose and fructose
(i) Glucose with acetic anhydride

(ii) Fructose with acetic anhydride

(iii)Glucose with HI

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(iv)Fructose with HI

(v)Glucose with phenyl hydrazine to form glucosazone

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(viii)fructose with hydroxylamine

+ H2O
(ix)glucose with bromine water

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(x)Fructose with bromine water --- No reaction
Test for glucose and fructose (bromine water test )
Glucose decolorizes the reddish brown color of bromine , whereas fructose does not .

(xi)Glucose with nitric acid

(xii)Fructose with nitric acid

Cyclic structure

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Disaccharides – structures of sucrose, maltose and lactose (glycosidic linkage).
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 C1 of α-D-glucose
and C2 of β-D-fructose. Since the reducing groups of glucose and fructose are involved in
glycosidic bond formation, sucrose is a non reducing sugar.

structures of lactose
Lactose: It is more commonly known as 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. Free aldehyde group may be produced at C-1 of glucose unit, hence it is also a reducing
sugar.

Maltose: Another 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.

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Proteins: are complex nitrogeneous organic compounds found in plants and animals. Some
proteins are enzymes which catalyse the biochemical reactions. Some are hormones which
regulate various biological activity.
Proteins are the most abundant biomolecules of the living system. Chief sources of proteins are
milk, cheese, pulses, peanuts, fish, meat, etc. They occur in every part of the body and form the
fundamental basis of structure and functions of life. They are also required for growth and
maintenance of body. All proteins are polymers of α-amino acids.
Amino acids –the organic molecules containing at least one carboxyllic group and one amino
group are called 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 α, β, γ, δ and so on. Only α-amino acids are obtained on hydrolysis of proteins. They
may contain other functional groups also. All α-amino acids have trivial names, which usually
reflect the property of that compound or its source. Glycine is so named since it has sweet taste (in
Greek glykos means sweet) and tyrosine was first obtained from cheese (in Greek, tyros means
cheese.)

general structure-

Classification :
(i) Acidic amino acids – These are amino acids having two carboxylic group and one amino
group per molecule . eg glutamic acid
(ii) Basic amino acids- These amino acids contain two or more amino groups and one
carboxylic group per molecule eg. Lysine
(iii) Neutral amino acids- These amino acids contain one amino group and one carboxylic
group per molecule. eg.glycine

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Zwitter ion formation.-The aqueous solution of amino acid is neutral and shows amphoteric
behavior. This is due to the formation of an internal salt called Zwitter ion .
In aqueous solution , the COOH group loses a proton which is taken up by the amino group .

Zwitter ion is neutral but contains both positive and negative charges . Due to its dipolar
nature it is reffered as dipolar ion .
In zwitter ion form , amino acids show amphoteric nature and react with both acids and bases
. In acidic solution , amino acids exists as positive ion and form salts with acids .
In basic solution , amino acids exists as negative ion and form salts with alkalis .

Isoelectric point-. In acidic solution , amino acids exists as positive ion and in basic solution,
amino acids exists as negative ion. On passing electric current , it will migrate towards the
cathode in acidic solution and towards anode in basic solution .Hence at a particular PH of
the solution , the amino acid molecule should not migrate towards either electrode and
should exists as a neutral diplor ion . This PH (6.3) is known as Isoelectric point.
Classification of proteins on the basis of molecular shape;
Fibrous proteins Globular proteins
Thread like structure Folded spheroidal structure
Polypeptide chains are held together by The intermolecular H- bonding is
stronger intermolecular H- bonds . comparatively weaker.
Insoluble in water soluble in water
Stable towards moderate changes in Very sensitive towards changes in
temperature and PH . temperature and PH.
Eg : Collagen – found in skin, bones, and Eg : Hemoglobin – found in red blood
connective tissues; provides structural cells; transports oxygen throughout the
support. body.

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 Structure of proteins
(i) Primary structure of proteins: 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. Any change in this primary structure i.e., the sequence of amino acids
creates a different protein.
(ii) Secondary structure of proteins: The secondary structure of protein refers to the
shape in which a long polypeptide chain can exist. They are found to exist in two
different types of structures viz. α-helix and β-pleated sheet structure. These structures
arise due to the regular folding of the backbone of the polypeptide chain due to
hydrogen bonding between and –NH– groups of the peptide bond. 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. In β-pleated sheet
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.
(iii) Tertiary structure of proteins: The tertiary structure of proteins represents overall
folding of the polypeptide chains i.e., further folding of the secondary structure. It gives
rise to two major molecular shapes viz. 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.
(iv) Quaternary structure of proteins: Some of the proteins are composed of two or more
polypeptide chains referred to as sub-units. The spatial arrangement of these subunits
with respect to each other is known as quaternary structure.

Summary
Primary Structure:The primary structure of a protein is the linear sequence of amino acids joined
by peptide bonds. This sequence determines the protein's overall structure and function.
Secondary Structure:The secondary structure refers to localized folding into alpha-helices or
beta-pleated sheets, stabilized by hydrogen bonds between backbone atoms. These structures
provide initial stability and shape to the protein chain.

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 Tertiary Structure:The tertiary structure is the three-dimensional shape formed by the folding
of the entire polypeptide chain, including interactions between side chains (R groups). It is
stabilized by hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions.
Quaternary Structure:The quaternary structure arises when two or more polypeptide chains
(subunits) associate to form a functional protein. The arrangement and interaction of these subunits
are crucial for the protein’s biological activity.
Peptide bonds
The definition of a polypeptide chain is a string of amino acids connected together by
peptide bonds. So, a polypeptide chain is a chain of the building blocks of proteins or amino
acids. Polypeptide chains are important because they make up proteins.
Denaturation of proteins: The process which leads to a change in the physical and
biological properties of a protein without affecting its chemical composition is called
Denaturation. During denaturation secondary and tertiary structures are destroyed but primary
structure remains intact. 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.
Methods of denaturation : By heat , alcohol, conc. acids , radiation etc.
Enzymes: are globular proteins which act as biocatalysts in the living system , produced by
living cells. For example, the enzyme that catalyses hydrolysis of maltose into glucose is
named as maltase.
Hormones are molecules that act as intercellular messengers. These are produced by
endocrine glands in the body and are poured directly in the blood stream which
transports them to the site of action. In terms of chemical nature, some of these are steroids,
e.g., estrogens and androgens; some are poly peptides for example insulin and endorphins and
some others are amino acid derivatives such as epinephrine and norepinephrine. They help to
maintain the balance of biological activities in the body.
Vitamins A, B, C, D, E and K: .
• Vitamins may be defined as a group of organic compounds which are required in very
small amounts for the healthy growth and normal functioning of living organisms.
• Classification of Vitamins –
(i) Fat Soluble – They are oily substances not readily soluble in water and are absorbed
by the body only when fat digestion and absorption proceed normally. Eg. Vitamin A, D,
E, K.
(ii) Water Soluble – They are soluble in water and are stored in lesser amounts in the
cells. Eg. Vitamin B, C.

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 Vitamin Deficiency diseases
Vitamin A Night blindness, xerosis(drying of skin)
xerophtalmia
Vitamin B Beriberi(paralysis of legs), loss of appetite,
anaemia , inflammation of tongue
Vitamin C Scurvy (bleeding of gums) , skin diseases
Vitamin D Rickets , deformation of bones and teeth
Vitamin E Sterility
Vitamin K haemorrhage
Nucleic acids: Nucleic acids are polymers of nucleotides, long thread like molecules present in
the nuclei of most living beings. Nucleotides are units of nucleic acid consisting of three parts –

A pentose sugar – ribose sugar , deoxyribose sugar and phosphate

- A nitrogenous base – (i) Purine: Adenine and Guanine(ii) Pyrimidine: Cytosine, Thymine
and Uracil .

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 β-D-
2-deoxyribose whereas in RNA molecule, it is β-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).

Types of Nucleic Acids –

(i) Deoxyribonucleic acid (DNA) – It is responsible for inheritance of genetic character.

(ii) Ribonucleic acid – It is of three types namely ribosomal RNA, messenger RNA and
transfer RNA.

Structure of nucleic acid

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.

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Nucleotides are joined together by phosphodiester linkage between 5′ and 3′ carbon atoms
of the pentose sugar.

DNA – structure (double helical),

• Each DNA molecule is made of two polynucleotide chains thus known as a double helical
structure. The purines are of two kinds (adenine and guanine) and the pyrimidines are
also of two kinds (cytosine and thymine). One of these bases is attached to the

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 deoxyribose sugar which is attached to the phosphate group. Two nitrogenous bases are
linked by a hydrogen bond and two sugar groups are linked by a phosphodiester bond.
The two chains of a DNA are called complimentary because a purine base is always
paired with a pyrimidine base.

Features of the DNA Double Helix

• Two DNA strands form a helical spiral, winding around a helix axis in a right-handed
spiral .The two polynucleotide chains run in opposite directions .The sugar-phosphate
backbones of the two DNA strands wind around the helix axis like the railing of a spiral
staircase.The bases of the individual nucleotides are on the inside of the helix, stacked on
top of each other like the steps of a spiral staircase.

• Two types of nucleic acids:

Deoxyribonucleic Acid (DNA) Ribonucleic Acid (RNA)

It has a double stranded α-helix structure in It has a single stranded α-helix structure.
which two strands are coiled spirally in
opposite directions.
Sugar present is β–D–2-deoxyribose Sugar present is β–D–ribose
Bases: Bases:
Purine bases: Adenine (A) and Guanine (G) Purine bases: Adenine (A) and Guanine (G)
Pyrimidine bases : Thymine (T) and cytosine Pyrimidine bases: Uracil (U) and cytosine
(C) (C)
It occurs mainly in the nucleus of the cell. It occurs mainly in the cytoplasm of the cell.
It is responsible for transmission for heredity It helps in protein synthesis.
character.
Biological Functions of Nucleic Acids : DNA is the chemical basis of heredity and may be
regarded as the reserve of genetic information. DNA is exclusively responsible for maintaining
the identity of different species of organisms over millions of years. A DNA molecule is capable
of self duplication during cell division and identical DNA strands are transferred to daughter
cells. Another important function of nucleic acids is the protein synthesis in the cell. Actually,
the proteins are synthesised by various RNA molecules in the cell but the message for the
synthesis of a particular protein is present in DNA.

1.What are monosaccharides?

2 What are reducing sugars?

3 Write two main functions of carbohydrates in plants.

4 Classify the following into monosaccharides and disaccharides. Ribose, maltose, galactose,
fructose and lactose.

5 What do you understand by the term glycosidic linkage?

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6 What is glycogen? How is it different from starch?

7 What are the hydrolysis products of (i) sucrose and (ii) lactose?

8 What is the basic structural difference between starch and cellulose?

9 (a) What happens when glucose is treated with the following reagents? (i) HI (ii) Bromine
water (iii) HNO3 (iv) Phenyl hydrazine (v) acetic anhydride

(b) What happens when fructose is treated with the following reagents? (i) HI (ii) Bromine water
(iii) HNO3 (iv) Phenyl hydrazine (v) acetic anhydride

10. What are essential and non-essential amino acids? Give two examples of each type.

11. Define the following as related to proteins (i) Peptide linkage (ii) Primary structure (iii)
Denaturation.

12. What are the common types of secondary structure of proteins?

13. What type of bonding helps in stabilising the α-helix structure of proteins?

14 Differentiate between globular and fibrous proteins.

15.How do you explain the amphoteric behaviour of amino acids?

16. What are enzymes?

17. What is the effect of denaturation on the structure of proteins?

18. How are vitamins classified? Name the vitamin responsible for the coagulation of blood.

19. Why are vitamin A and vitamin C essential to us? Give their important sources.

20. What are nucleic acids? Mention their two important functions.

21. The two strands in DNA are not identical but are complementary. Explain.

22. Write the important structural and functional differences between DNA and RNA.

23. What are the different types of RNA found in the cell?

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