Biomolecule
Biomolecule
Biomolecules
1. Biomolecules: Macromolecules which are naturally occurring in biological systems are called
biomolecules. Examples: polysaccharides (starch, cellulose, etc.), proteins, enzymes, vitamins, hormones,
etc.
2. Carbohydrates: These are optically active polyhydroxy aldehydes or ketones or the compounds which
produce such units on hydrolysis, e.g., glucose, sucrose, cellulose, starch, etc.
3. Classification of carbohydrates:
(a) Monosaccharides: The simple carbohydrates that cannot be broken further into smaller units on
hydrolysis, e.g., glucose and fructose, ribose, etc.
(b) Oligosaccharides: These are the carbohydrates which on hydrolysis give two to ten units of
monosaccharides, e.g., sucrose, maltose, raffinose, stachyose, etc.
(c) Polysaccharides: These are the carbohydrates which produce a large number of monosaccharide units
on hydrolysis, e.g., starch, cellulose, etc.
Importance of carbohydrates:
(i) Carbohydrates act as biofuel to provide energy for functioning of living systems.
C6 H12 O6 + 6O 2 6CO 2 + 6H 2 O + 2832 kJ
(ii) Carbohydrates are used as storage molecules as starch in plants and glycogen in animals.
(iii) D-Ribose and 2-Deoxy-D-ribose are present in RNA and DNA, respectively.
(iv) Cellulose acts as structural material of cell walls of bacteria and plants.
(v) Carbohydrates provide raw material for many important industries like textiles, paper, lacquers and
breweries.
4. (i) Reducing sugars: Those carbohydrates which contain free aldehydic or ketonic group and reduce
Fehling’s solution and Tollens’ reagent are called reducing sugars, e.g., all monosaccharides, maltose
and lactose.
(ii) Non-reducing sugars: Those sugars which do not have free aldehydic or ketonic group and do not
reduce Fehling’s solution or Tollens’ reagent are called non-reducing sugars, e.g., sucrose.
5. Preparation of Glucose
(a) From sucrose:
+
H
C12 H 22 O11 + H2 O C6 H12 O6 + C6 H12 O6
Sucrose Glu cos e Fructose
Biomolecules 563
(b) From starch: Commercially, glucose is obtained by hydrolysis of starch by boiling it with dil. H2SO4 at
393 K under pressure.
+
H
(C6 H10 O5) n + nH 2 O nC6 H12 O6
393K; 2 - 3 atm
Starch or cellulose Glucose
6. (a) Structure of Glucose: Glucose is a six carbon straight chain aldose which has one aldehydic group
(—CHO), one primary hydroxyl group (—CH2OH) and four secondary hydroxyl groups (—CHOH).
If the —OH group attached to C-5 is on the right side, the glucose is assigned D–configuration; if the
—OH group attached to C-5 is on the left side, it is assigned L–configuration. The (+) and (–) signs
represent the optical rotation as dextro and laevo, respectively and have no relationship with D and L
configuration.
CHO CHO
H OH HO H
HO H H OH
CHO H OH HO H
CHO
H OH H OH HO H
OH H
CH2OH CH2OH CH2OH CH2—OH
D-(+)-Glyceraldehyde
D-(+)-Glucose L-(–)-Glyceraldehyde L-(–)-Glucose
(b) Cyclic structure of glucose: The glucose has been shown to possess cyclic structure represented as
follows:
O
1 1 1
H C OH H C HO C H
2 2 2
H OH H OH H OH
O O
3 3 3
HO H HO H HO H
4 4 4
H OH H OH H OH
5 5 5
H H OH H
6 6 6
CH2OH CH2OH CH2OH
α-D-(+)-Glucose β-D-(+)-Glucose
Haworth Structures
6 CH2OH 6 CH2OH
5 O 5 O
O H H H OH
H H
4 1 4 1
OH H OH H
HO OH HO H
3 3
2 2
Pyran
H OH H OH
α-D-(+)-Glucopyranose β-D-(+)-Glucopyranose
CH2OH
Glucose cyanohydrin
HCN
COOH CHO
HNO3 HI
(CHOH)4 (CHOH)4 CH3 CH2 CH2 CH2 CH2 CH3
n-Hexane
COOH CH2OH
Saccharic acid Glucose Br
wa
OH
2
ter
Acetic anhydride
2—
COOH
NH
CH—N—OH (CHOH) 4
(CHOH)4 CH2OH
Gluconic acid
CHO O
CH2OH
Glucose oxime
(CH—O—C—CH3)4
O
CH2—O—C—CH3
Glucose pentaacetate
8. Structure of Fructose: Fructose is a ketohexose and has the molecular formula C6H12O6. It belongs to
D-series and is a laevorotatory compound.
2 1
1 2 HO C CH2OH
HOH2 C C OH 3
3 HO H
O HO H O
O 4
4 H OH
H OH
5
5 H
H 6
6 CH2OH
CH2OH
Furan α-D-(–)-Fructofuranose β-D-(–)-Fructofuranose
The cyclic structures of two anomers of fructose are represented by Haworth structures as given below.
6 1 6
HOH2C CH2OH HOH2C OH
5 2 5 2
H OH H OH
H 4 3 OH H 4 3 CH2OH
1
OH H OH H
α-D-(– )-Fructofuranose β-D-(–)-Fructofuranose
9. Disaccharides: The sugar which on hydrolysis gives two units of monosaccharides is called disaccharide.
Disaccharides are crystalline solids and are soluble in water. Sucrose, maltose and lactose are disaccharides.
Hydrolysis of sucrose is called inversion of cane sugar. Sucrose is a disaccharide because on hydrolysis, it
produces two monosaccharides namely D-(+)-glucose and D-(–)-fructose.
+
H
C12 H 22 O11 + H2 O C6 H12 O6 + C6 H12 O6
Sucrose D - (+) - Glucose D - (–) - Fructose
(disaccharide) (monosaccharide) (monosaccharide)
Biomolecules 565
(a) Ring structure of a sucrose molecule: A sucrose molecule is composed of a-glucose and b-fructose
units.
6
CH2OH
O 1 O
5
H H HOH2C H
H
4 1 2 5
OH H O H HO
HO 3 2 3 4 CH2OH
6
Glycosidic
linkage H
H OH OH
α-D-Glucose β-D-Fructose
Sucrose
(b) Ring structure of a maltose molecule: A maltose molecule is composed of two a-D-glucose units in
which C-1 of one glucose (I) is linked to C-4 of another glucose unit (II).
6 6
CH2OH CH2OH
5 O 5 O
H H H H
H H
4 1 4 1
OH H O OH H
HO 3 2 3 2 OH
H OH H OH
α-D-Glucose α-D-Glucose
I Maltose II
(c) Ring structure of a lactose molecule: A lactose molecule is composed of b-D-galactose and
b-D-glucose units.
6 6
CH2OH CH2OH
5 O 5 O
HO H OH
H H
4 1 4 1
OH H O OH H
H 3 2 H 3 2 H
H OH H OH
β-D-Galactose β-D-Glucose
Lactose
10. Polysaccharides: Polysaccharides are the carbohydrates which yield a large number of monosaccharide
molecules upon hydrolysis. Starch, cellulose and glycogen are examples of polysaccharides.
(a) Starch: The fundamental unit of starch is a-D-glucose.
Structure of starch: Starch is a polymer of a-glucose and consists of two components—amylose
and amylopectin. Amylose is a long unbranched chain with 200–1000 a-D-(+)-glucose units held by
C1–C4 glycosidic linkage.
6
CH2OH CH2OH CH2OH
O 5 O O
H H H H H H H H H
4 1 4 1 4 1
O OH H O OH H O OH H O
3 2
H OH H OH H OH
α-Link α-Link
Amylose
Amylopectin is a branched chain polymer of a-D-glucose units in which the chain is formed by C1–C4
glycosidic linkage, whereas branching occurs by C1–C6 glycosidic linkage.
H OH H OH O
α-Link Branch at C6
H OH H OH H OH
α-Link α-Link
Amylopectin
(b) Cellulose: Cellulose is a polysaccharide. The fundamental structural unit of cellulose is b-D-glucose.
Structure of cellulose: Cellulose is a linear polymer of b-D-glucose which are joined by glycosidic
linkage between C1 of one glucose unit and C4 of the next glucose unit.
HOH2C
O
O
OH
HOH2C O OH
O
OH
HOH2C O OH
O
β-links
OH
Cellulose
O
OH
11. Amino acids: Those compounds, whose molecule contains both the carboxylic acid group and the amino
group are called amino acids. There are twenty amino acids which form protein. The amino acids which
are synthesised in body are known as non-essential amino acids, e.g., glycine, alanine. Those amino acids
which cannot be synthesised in body and must be obtained through diet are known as essential amino acids,
e.g., valine, lysine.
Amino acids have also been classified as neutral, acidic and basic amino acids. Amino acids like glycine,
valine, etc. which contain one —NH2 and one —COOH group are called neutral amino acids. Those amino
acids such as aspartic acid, glutamic acid, etc. which contain one —NH2 group and two —COOH groups
are called acidic amino acids and amino acids such as lysine, histidine, etc., which contain two —NH2
groups and one —COOH group are called basic amino acids.
12. Proteins are complex nitrogenous organic molecules which are essential for growth and maintenance of body.
O
||
Chemically, proteins are the polymers of a-amino acids which are linked by peptide bonds (—C—NH—) .
Biomolecules 567
(a) Types of proteins based on molecular shape:
(i) Fibrous proteins: They have thread-like molecules which tend to lie side by side to form fibres,
e.g., keratin, collagen, myosin, fibroin, etc. In such proteins, the molecules are held together by
hydrogen and disulphide bonds. They are insoluble in water. They are the chief structural materials
of animal tissues.
(ii) Globular proteins: They have molecules which are folded into compact units that often form
spheroidal shapes. The area of contact between molecules are small and inter-molecular forces
are comparatively weak, e.g., insulin, thyroglobulin, albumin, haemoglobin and fibrinogen. In
clotting of blood, fibrinogen gets converted into fibrous protein, fibrin.
(b) Structure of Proteins: There are four levels at which the structure of proteins are studied. These are
primary, secondary, tertiary and quarternary levels.
(i) Primary structure of proteins: The sequence in which various amino acids are arranged in a
protein is called its primary structure. Any change in the sequence of amino acids creates different
protein which alters biological functions.
(ii) Secondary structure of proteins: It refers to shape in which a long polypeptide chain exists. A
protein may assume a-helix structure or b-pleated sheet structure. The a-helix structure results due
to regular coiling of polypeptide chain which is stabilised by intramolecular hydrogen bonding.
Keratin in hair, nails, wool and myosin in nucleus have a-helix structure. In b-pleated sheet
structure, all peptide chains are stretched to nearly maximum extension and then arranged side by
side and held together by intermolecular hydrogen bonding. Silk has b-pleated sheet structure.
(iii) Tertiary structure of proteins: The tertiary structure of proteins represents overall folding of the
polypeptide chain, 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 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals forces and electrostatic force of attraction.
(iv) Quaternary structure: 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.
(c) Denaturation of Proteins: When a protein in its native form is subjected to a change, such as change
in temperature or 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. During
denaturation, 2° and 3° structures are destroyed but 1° structure remains intact, e.g., coagulation of egg
while on boiling, curdling of milk, etc.
13. (a) Enzymes: Enzymes are essential biological catalysts which are required to catalyse biological
reactions, e.g., maltose, lactose, invertase, etc. Almost all the enzymes are globular proteins.
(b) Oxidoreductase enzymes: Enzymes which catalyse the oxidation of one substrate with simultaneous
reduction of another substrate.
(c) Phenylketonuria: Disease caused by deficiency of the enzyme phenylalanine hydroxylase.
(d) Albinism: Disease caused due to deficiency of an enzyme tyrosinase.
(e) Streptokinase: Enzyme which dissolves the blood clot formed in coronary artery which leads to heart
trouble.
14. Nucleic Acids: Nucleic acids are long chain polymers of nucleotides. They play an important role in
transmission of hereditary characteristics and biosynthesis of proteins.
Types of nucleic acids: There are two types of nucleic acids. These are DNA and RNA.
(a) Constituents of nucleic acids:
(i) Pentose sugar (ii) Phosphoric acid (iii) Nitrogenous bases.
In DNA, b-D-2-deoxyribose sugar is present while in RNA b-D-ribose sugar is present.
Nitrogen containing bases: There are two types of nitrogen containing bases found in nucleic acids.
These are pyrimidines and purines.
Pyrimidines: There are three bases derived from pyrimidines. These are cytosine (C), thymine (T)
and uracil (U). In DNA, T is present but in RNA, U is present.
Purines: There are two bases derived from purine. These are adenine (A) and guanine (G).
3'
OH OH
3' end of chain
Formation of dinucleotide
(b) Deoxyribonucleic acid (DNA): It contains a pentose sugar deoxyribose, and adenine, guanine,
thymine and cytosine bases. A phosphate group is present at C-5 of the sugar unit. The repeating
units, deoxyribonucleotides, are linked by phosphate group. Thus, they are the biopolymers of
deoxyribonucleotides and have double helix structure of polynucleotides. The two strands of DNA
are said to be complementary to each other. Adenine forms hydrogen bonds with thymine whereas
cytosine forms hydrogen bonds with guanine. They are responsible for genetic characteristics and for
sending information and instruction in the cell for the synthesis of specific protein.
(c) Ribonucleic acid (RNA): It contains ribose sugar, bases from pyrimidine bases—uracil and cytosine,
and two bases from purine base—adenine and guanine. A phosphate group is present at C-5 of the
sugar unit. The repeating units, ribonucleotides, are linked by phosphate group. They are the polymers
of ribonucleotide and have a single helix structure. RNA is associated with the process of learning and
memory storage, and helps in biosynthesis of protein.
15. Functions of Nucleic Acids: Two main functions of nucleic acids are:
(a) Replication or heredity transfer: The double helix of DNA is the storehouse of the genetic
information of the organism which is contained in the sequence of bases A, T, C, G on the strands of
DNA. The process by which a DNA molecule produces two identical molecules of itself in the nucleus
of the cell is called replication.
Biomolecules 569
(b) Protein synthesis: This is brought about in two steps:
(i) Transcription: Copying of sequence of bases from the DNA strand onto the RNA molecule is
called transcription. During transcription, the double helix of the DNA partially unwinds and one
of the two DNA strands serves as a template for the synthesis of RNA strand called messenger
RNA (mRNA) which is complementary to a segment of the DNA chain.
(ii) Translation: This is the process in which mRNA directs protein synthesis in the cytoplasm of cell
with involvement of transfer RNA (tRNA) and ribosomal particles (rRNA protein complexes).
16. (a) Codon: The sequence of nucleotides in mRNA molecules are read in a serial order in sets of three
(triplet) at a time. Each triplet is called a codon. It specifies one amino acid. The mRNA codon
recognises the amino acids through tRNAs which carry specific amino acids.
(b) Gene: The sequence of bases or nucleotides in the DNA molecule which regulates the synthesis of a
specific protein is called a gene. Every protein in the cell has a corresponding gene. The relationship
between a nucleotide triplet (codon) and the amino acid is called genetic code.
(c) Mutation: The chemical change in the sequence of bases in the DNA molecule can lead to synthesis
of protein with an altered amino acid sequence is called mutation. This is brought about spontaneously
by exposure to UV-rays, X-rays and chemicals.
17. Vitamins: Vitamins are generally regarded as 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.
Vitamins are classified into two groups depending upon their solubility in fat or water:
(i) Fat-soluble vitamins: Vitamins A, D, E and K are soluble in fat and oils but insoluble in water. They
are stored in liver and adipose tissues.
(ii) Water-soluble vitamins: Vitamins belonging to group B and vitamin C are soluble in water. They
must be supplied regularly in diet because they are readily excreted in urine and cannot be stored
(except vitamin B12) in our body.
Table 14.1: Some Important Vitamins, their Sources and their Deficiency Diseases
S. No. Name of Vitamins Sources Deficiency Diseases
1. Vitamin A Fish liver oil, carrots, butter Xerophthalmia (hardening of cornea of eye), night
and milk blindness
2. Vitamin B1 (Thiamine) Yeast, milk, green Beri-beri (loss of appetite, retarded growth)
vegetables and cereals
3. Vitamin B2 (Riboflavin) Milk, egg white, liver, Cheilosis (fissuring at corners of mouth and lips),
kidney digestive disorders and burning sensation of the
skin.
4. Vitamin B6 (Pyridoxine) Yeast, milk, egg yolk, Convulsions
cereals and grams
5. Vitamin B12 Meat, fish, egg and curd Pernicious anaemia (RBC deficient in haemoglobin)
6. Vitamin C Citrus fruits, amla and Scurvy (bleeding gums)
(Ascorbic acid) green leafy vegetables.
7. Vitamin D Exposure to sunlight, fish Rickets (bone deformities in children) and
and egg yolk osteomalacia (soft bones and joint pain in adults)
8. Vitamin E Vegetable oils like wheat Increased fragility of RBCs and muscular weakness
germ oil, sunflower oil, etc.
9. Vitamin K Green leafy vegetables Increased blood clotting time
18. Hormones: Hormones are molecules that act as intercellular messengers. These are produced by endocrine
glands in the body and are released directly in the blood stream. From here these are transported to the site
of their action.
Functions of hormones:
(i) They help to maintain the balance of biological activities in the body. For example, insulin keeps the
blood glucose level within the range, epinephrine and norepinephrine mediate response to external
stimuli, growth hormones and sex hormones play role in growth and development.
CH==NOH
NH2OH
H OH
HO H
H OH
No oxime
H OH
CH2OH
Glucose oxime
Biomolecules 571
Q. 4. The melting points and solubility in water of amino acids are generally higher than that of the
corresponding halo acids. Explain.
+
Ans. The amino acids exist as zwitter ions, H3N—CHR—COO–. Because of this dipolar salt-like character,
they have strong dipole–dipole attractions. So, their melting points are higher than halo acids which do not
have salt-like character. Moreover, due to this salt-like character, they interact strongly with H2O. Thus,
solubility in water of amino acids is higher than that of the corresponding halo acids which do not have
salt-like character.
Q. 5. Where does the water present in the egg go after boiling the egg?
Ans. On boiling the egg, the proteins undergo denaturation and the water present in the egg gets absorbed or
adsorbed in the denaturated proteins probably through H-bonding.
Q. 6. Why cannot vitamin C be stored in our body?
Ans. Vitamin C is soluble in water, hence, it is readily excreted in urine and thus cannot be stored in the body.
Q. 7. What products would be formed when a nucleotide from DNA containing thymine is hydrolysed?
Ans. Besides thymine, the two products are 2-deoxy-D-ribose and phosphoric acid.
Q. 8. When RNA is hydrolysed, there is no relationship among the quantities of different bases obtained.
What does this fact suggest about the structure of RNA? [HOTS]
Ans. A DNA molecule has two strands in which the four complementary bases pair each other, viz., cytosine (C)
always pairs with guanine (G) while thymine (T) always pairs with adenine (A). Therefore, when a DNA
molecule is hydrolysed, the molar amounts of cytosine is always equal to that of guanine and that of
adenine is always equal to that of thymine. RNA also contains four bases, the first three are same as in DNA
but the fourth one is uracil (U).
As in RNA, there is no relationship between the quantities of four bases (C, G, A and U) obtained, therefore,
the base-pairing principle, viz., A pairs with U and C pairs with G is not followed. So, unlike DNA, RNA
has a single strand.
Q. 8. What is the basic structural difference between starch and cellulose? [CBSE 2019 (56/2/2)]
OR
Starch and cellulose both contain glucose units as monomer, yet they are structurally different.
Explain. [CBSE 2020 (56/1/2)]
Ans. Starch consists of amylose and amylopectin.
Amylose is a long unbranched chain with a-D(+)-glucose units that are held together with C1–C4 glycosidic
linkage. Amylopectin is a highly branched chain polymer of a-D-glucose units in which glycosidic linkage
is present between C1–C4 atoms and branching occurs through C1–C6 glycosidic linkage. For figures
refer to Basic Concept Point 10(a).
Cellulose is a straight chain polysaccharide composed only of b-D-glucose units which are joined by
glycosidic linkage between C1 of one glucose units and C4 of next glucose units. For figure refer to Basic
Concepts Point 10(b).
Q. 9. What happens when D-glucose is treated with the following reagents? [CBSE 2019 (56/5/2)]
(i) HI (ii) Bromine water (iii) HNO3
Ans. Refer to Basic Concepts Point 7.
Q. 10. Enumerate the reactions of D-glucose which cannot be explained by its open chain structure.
Ans. The following reactions cannot be explained by its open chain structure proposed by Baeyer:
(i) Despite having an aldehydic group, glucose does not give Schiff’s test and it does not react with
sodium bisulphite and ammonia.
(ii) The pentaacetate of glucose does not react with hydroxylamine indicating absence of —CHO group.
(iii) When D-glucose is treated with methyl alcohol in presence of dry hydrogen chloride gas, it gives
two isomeric mono methyl derivatives known as a-D-glucoside and methyl b-D-glucoside. These
glucosides does not reduce Fehling’s solution and also do not react with hydrogen cyanide or
hydroxylamine indicating the absence of free —CHO group.
Q. 11. What are essential and non-essential amino acids? Give two examples of each type.
[CBSE Delhi 2010]
Ans. a-Amino acids which are required for health and growth of human beings but are not synthesised by the
human body are known as essential amino acids. Examples: valine, leucine, phenylalanine, etc. On the
other hand, a-amino acids which are needed for health and growth of human beings and are synthesised by
the human body are called non-essential amino acids. Examples: glycine, alanine, aspartic acid, etc.
Q. 12. Define the following terms as related to proteins:
(i) Peptide linkage (ii) Primary structure (iii) Denaturation
[CBSE (AI) 2014; 2019 (56/5/2)]
O
||
Ans. (i) A peptide linkage is an amide (—C—NH—) linkage formed between —COOH group of one
a-amino acid and —NH2 group of other a-amino acid by loss of a water molecule.
(ii) The specific sequence in which various a-amino acids present in a protein are linked to one another
is called its primary structure. Any change in its primary structure creates a new protein.
(iii) When a protein in its native form is subjected to a change, such as change in temperature or 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. During denaturation, 2° and 3°
structures are destroyed but 1° structure remains intact, e.g., coagulation of egg while on boiling,
curdling of milk, etc.
Biomolecules 573
Q. 13. What are common types of secondary structure of proteins?
Ans. The conformation which the polypeptide chains assume as a result of hydrogen bonding is known as the secondary
structure of the proteins. The two types of secondary structures are a-helix and b-pleated sheet structure.
Q. 14. What type of bonding helps in stabilising the a-helix structure of proteins?
Ans. The a-helix structure of proteins is stabilised by intramolecular H-bonding between C—O of one amino
acid residue and the N—H of the fourth amino acid residue in the chain.
Q. 15. Differentiate between globular and fibrous proteins. [CBSE 2019 (56/5/2), 2020 (56/5/1)]
Ans. Refer to Basic Concepts Point 12(a).
Q. 16. How do you explain the amphoteric behaviour of amino acids?
Ans. Amino acids contain 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 with both acids and bases.
O O
|| ||
R— CH— C—O—H R— CH— C—O –
| |
:: NH 2 +
NH3
Q. 17. What are enzymes?
Ans. Enzymes are biological catalysts. Each biological system requires a different enzyme. So, as compared to
conventional catalysts, enzymes are specific and efficient in their action. They are required in only small
quantity and work at optimum temperature (310 K) and pH (7.4) under 1 atmospheric pressure. Chemically,
they are globular proteins. However, some enzymes are also associated with some non-protein components
called the co-factors for their activity. Cofactors are of two types:
(i) Inorganic ions such as Zn2+, Mg2+, Mn2+, Fe2+, Cu2+, Co2+, etc.
(ii) Organic molecules: These are of two types:
(a) Coenzymes: These are usually derived from vitamins such as thymine, riboflavin, niacin, etc. They
are loosely held to the protein and can be easily separated by dialysis.
(b) Prosthetic group: They are also derived from vitamins such as biotin but are tightly held to the
protein molecule by covalent bonds. They can be separated only by careful hydrolysis.
Q. 18. What is the effect of denaturation on the structure of proteins?
Ans. During denaturation, 2° and 3° structures of proteins are destroyed but 1° structure remains intact. Due to
denaturation, the globular proteins (soluble in H2O) are converted into fibrous proteins (insoluble in H2O) and
their biological activity is lost. For example, boiled egg which contains coagulated proteins cannot be hatched.
Q. 19. How are vitamins classified? Name the vitamin responsible for the coagulation of blood.
Ans. Vitamins are classified into two groups depending upon their solubility in water or fat.
(i) Water-soluble vitamins: These include vitamin B-complex (B1, B2, B5, i.e., nicotinic acid, B6, B12,
pantothenic acid, biotin, i.e., vitamin H and folic acid) and vitamin C.
(ii) Fat-soluble vitamins: These include vitamin A, D, E and K. These are stored in liver and adipose
tissues (fat storing tissues).
Vitamin K is responsible for coagulation of blood.
Q. 20. Why are vitamin A and vitamin C essential to us? Give their important sources.
Ans. Vitamin A is essential for us because its deficiency can cause xerophthalmia (hardening of cornea of eye)
and night blindness.
Sources: Carrots, fish liver oil, butter and milk.
Vitamin C: Vitamin C is essential for us because its deficiency causes scurvy (bleeding gums) and pyorrhea
(loosening and bleeding of teeth).
Sources: Amla, citrus fruits and green leafy vegetables.
Q. 21. What are nucleic acids? Mention their two important functions.
Ans. Nucleic acids are biomolecules which are found in the nuclei of all living cells in the form of nucleoproteins
or chromosomes (proteins containing nucleic acids as the prosthetic group).
H
T A N
G C H
34Å A T
T A 3.4Å
N N
C O
Pentose
sugar H
O N
A T N
T A
C G H N
G C Hydrogen bond N N
H Pentose
sugar
5′ 3′
20Å
(a) The double strand helix structure for DNA (b) Base pair in DNA
Biomolecules 575
Q. 24. Write the important structural and functional differences between DNA and RNA.
Ans.
Structural differences
DNA RNA
(i) The sugar present in DNA is 2-deoxy-D-(–)-ribose. The sugar present in RNA is D-(–)-ribose.
(ii) DNA contains cytosine and thymine as pyrimidine RNA contains cytosine and uracil as pyrimidine
bases. bases.
(iii) DNA has a double stranded a-helix structure. RNA has a single stranded a-helix structure.
(iv) DNA molecules are very large; their molecular mass RNA molecules are much smaller with molecular
may vary from 6 × 106 – 16 × 106 u. mass ranging from 20,000 to 40,000 u.
Functional differences
(i) DNA has unique property of replication. RNA usually does not replicate.
(ii) DNA controls the transmission of hereditary effects. RNA controls the synthesis of proteins.
Q. 25. What are the different types of RNA found in the cell? [CBSE Delhi 2013]
Ans. There are three types of RNAs:
(i) Ribosomal RNA (rRNA) (ii) Messenger RNA (mRNA) (iii) Transfer RNA (tRNA)
1. Three cyclic structures of monosaccharides are given below which of these are anomers.
[NCERT Exemplar]
HO H
H OH HO H HO H
H OH H OH HO H
O O O
HO H HO H H OH
H OH H OH HO H
H H H
H OH HO H H OH HO H
H OH H OH H OH HO H
(c) O O (d) O O
HO H HO H HO H H OH
H OH H OH H OH HO H
H H H H
CH2OH CH2OH CH2OH CH2OH
7. Fructose reduces Tollens’ reagent due to
(a) Primary alcoholic group (b) Asymmetric carbons
(c) Secondary alcoholic groups (d) Enolisation of fructose followed by conversion to
aldehyde by base
8. Carbohydrates are classified on the basis of their behaviour on hydrolysis and also as reducing or
non-reducing sugar. Sucrose is a __________.[NCERT Exemplar]
(a) monosaccharide (b) disaccharide
(c) reducing sugar (d) non-reducing sugar
9. Amylopectin is insoluble in water and constitutes about
(a) 15–20% of starch (b) 20–40% of starch (c) 50–70% of starch (d) 80–85% of starch
10. Cellulose is not digestible by human beings due to absence of cellulose hydrolysing enzyme called
(a) cellulase (b) invertase (c) zymase (d) urease
11. Glycogen is a branched chain polymer of α-D-glucose units in which chain is formed by C1—C4
glycosidic linkage whereas branching occurs by the formation of C1—C6 glycosidic linkage.
Structure of glycogen is similar to __________. [NCERT Exemplar]
(a) Amylose (b) Amylopectin (c) Cellulose (d) Glucose
12. Which of the following polymer is stored in the liver of animals?[NCERT Exemplar]
(a) Amylose (b) Cellulose (c) Amylopectin (d) Glycogen
13. Which of the following naturally occurring a – aminoacids is optically inactive?
(a) Glycine (b) Alanine (c) Leucine (d) Valine
Biomolecules 577
14. Each polypeptide in a protein has aminoacids linked with each other in a specific sequence. This
sequence of amino acids is said to be __________.[NCERT Exemplar]
(a) primary structure of proteins. (b) secondary structure of proteins.
(c) tertiary structure of proteins. (d) quaternary structure of proteins.
15. Proteins can be classified into two types on the basis of their molecular shape i.e., fibrous proteins and
globular proteins. Examples of globular proteins are :[NCERT Exemplar]
(a) Insulin (b) Keratin (c) Albumin (d) Myosin
16. Proteins are found to have two different types of secondary structures viz. α-helix and β-pleated
sheet structure. α-helix structure of protein is stabilised by :[NCERT Exemplar]
(a) Peptide bonds (b) van der Waals forces (c) Hydrogen bonds (d) Dipole-dipole interactions
17. Which of the following B group vitamins can be stored in our body?[NCERT Exemplar]
(a) Vitamin B1 (b) Vitamin B2 (c) Vitamin B6 (d) Vitamin B12
18. Which of the following acids is a vitamin?[NCERT Exemplar]
(a) Aspartic acid (b) Ascorbic acid (c) Adipic acid (d) Saccharic acid
19. Nucleic acids are the polymers of __________.[NCERT Exemplar]
(a) nucleosides (b) nucleotides (c) bases (d) sugars
20. Dinucleotide is obtained by joining two nucleotides together by phosphodiester linkage. Between
which carbon atoms of pentose sugars of nucleotides are these linkages present? [NCERT Exemplar]
(a) 5′ and 3′ (b) 1′ and 5′ (c) 5′ and 5′ (d) 3′ and 3′
21. DNA and RNA contain four bases each. Which of the following bases is not present in RNA?
[NCERT Exemplar]
(a) Adenine (b) Uracil (c) Thymine (d) Cytosine
22. The presence or absence of hydroxyl group on which carbon atom of sugar differentiate RNA and DNA
(a) 2nd (b) 4th (c) 3rd (d) 1st
23. Which one is the complementary base of cytosine in one strand to that in other strand of DNA?
[CBSE 2020 (56/4/3)]
(a) Adenine (b) Guanine (c) Thymine (d) Uracil
Answers
1. (a) 2. (a) 3. (c) 4. (c) 5. (d) 6. (c) 7. (d) 8. (b, d) 9. (d) 10. (a)
11. (b) 12. (d) 13. (a) 14. (a) 15. (a, c) 16. (c) 17. (d) 18. (b) 19. (b) 20. (a)
21. (c) 22. (a) 23. (b)
Assertion-Reason Questions
In the following questions, two statements are given—one labeled Assertion (A) and the other labeled
Reason (R). Select the correct answer to these questions from the codes (a), (b), (c) and (d) as given below:
(a) Both Assertion (A) and Reason (R) are correct statements, and Reason (R) is the correct explanation of
the Assertion (A).
(b) Both Assertion (A) and Reason (R) are correct statements, but Reason (R) is not the correct explanation
of the Assertion (A).
(c) Assertion (A) is correct, but Reason (R) is incorrect statement.
(d) Assertion (A) is incorrect, but Reason (R) is correct statement.
1. Assertion (A) : Deoxyribose, C5H10O4 is a carbohydrate.
Reason (R) : Carbohydrates are hydrates of carbon so compounds which follow Cx(H2O)y formula are
carbohydrates.
2. Assertion (A) : D (+) – Glucose is dextrorotatory in nature.
Reason (R) : ‘D’ represents its dextrorotatory nature.
Reason (R) : Maltose is composed of two glucose units in which C1 of one glucose unit is linked to C4
of another glucose unit.
7. Assertion (A) : All naturally occurring α-aminoacids except glycine are optically active.
Reason (R) : Most naturally occurring amino acids have L-configuration.
8. Assertion (A) : Glycine must be taken through diet.
Reason (R) : It is a non-essential amino acid.
9. Assertion (A) : Proteins are made up of a-amino acids.
Reason (R) : During denaturation, secondary and tertiary structures of proteins are destroyed.
10. Assertion (A) : In presence of enzyme, substrate molecule can be attacked by the reagent effectively.
Reason (R) : Active sites of enzymes hold the substrate molecule in a suitable position.
11. Assertion (A) : Vitamin D can be stored in our body.
Reason (R) : Vitamin D is fat soluble vitamin.
Answers
1. (c) 2. (c) 3. (a) 4. (a) 5. (c) 6. (d) 7. (b) 8. (d) 9. (b) 10. (a)
11. (a)
Passage-based/Case-based Questions
Read the given passages and answer the questions that follow.
PASSAGE–1
The most abundant biomolecules of the living system are proteins. They are polymers of a-amino acids
connected to each other by peptide linkage. Amino acids contain amino (—NH2) and carboxyl (—COOH) group.
Amino acids are classified as acidic, basic or neutral depending upon the relative number of amino and carboxyl
groups in their molecule. They behave like salts rather than simple amines or carboxylic acids. 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.
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.
Biomolecules 579
1. The Ka and Kb values of a-amino acid are very low. Why?
+
Ans. In a-amino acids the acidic group is —NH3, instead of —COOH group as in carboxylic acids and basic
group is —COO– instead of —NH2 group as in amines. That is why they have low values of Ka and Kb.
2. Draw the structure of zwitter ion.
O O
|| ||
Ans. R—CH— C —OH R—CH—C—O –
| |
NH 2 NH3
+
(Zwitter ion)
PASSAGE–2
Carbohydrates, proteins, nucleic acids, etc. form the basis of life and are responsible for the growth and
maintenance of living systems. Therefore, they are referred to as biomolecules. Carbohydrates are widely distributed
in nature. Carbohydrates are optically active polyhydroxy aldehydes or ketones or the compounds which produce such
units on hydrolysis. Glucose, fructose, sucrose, starch, cellulose, etc. are some naturally occurring carbohydrates.
They act as the major source of energy for animals and human beings.
Monosaccharides are the simple carbohydrates that cannot be broken further into smaller units on hydrolysis,
e.g., glucose and fructose, ribose, etc. Oligosaccharides are the carbohydrates which on hydrolysis give two to ten
units of monosaccharides, e.g., sucrose, maltose, raffinose, stachyose, etc. Polysaccharides are the carbohydrates
which produce a large number of monosaccharide units on hydrolysis, e.g., starch, cellulose, etc.
1. Which carbohydrate provides instant energy to the body?
Ans. Glucose
2. Which disaccharide is found only in animals and not in plants?
Ans. Lactose
3. Which carbohydrate is the main constituent of plant cell wall?
Ans. Cellulose
4. Write the name of two monosaccharides obtained on hydrolysis of lactose sugar.
Ans. D-(+)-Glucose and D-(+)-Galactose
5. Which one of the following is a polysaccharide?
Starch, Maltose, Fructose, Glucose
Ans. Starch
Biomolecules 581
Q. 2. How do you explain the presence of an aldehydic group in a glucose molecule? [NCERT Exemplar]
Ans. Glucose reacts with hydroxylamine to form a monoxime and adds one molecule of hydrogen cyanide to
give cyanohydrin so it contains a carbonyl group which can be an aldehyde or a ketone. On mild oxidation
with bromine water, glucose gives gluconic acid which is a six carbon carboxylic acid. This indicates that
carbonyl group present in glucose is an aldehydic group.
Q. 3. Label the glucose and fructose units in the following disaccharide and identify anomeric carbon
atoms in these units. Is the sugar reducing in nature? Explain. [NCERT Exemplar] [HOTS]
CH2OH
O O
H H HOH2C H
H
OH H O H HO
HO CH2OH
H OH OH H
Ans. C-l of glucose unit and C-2 of fructose unit are anomeric carbon atoms in the given disaccharide. The
disaccharide is non-reducing sugar because —OH groups attached to anomeric carbon atoms are involved
in the formation of glycosidic bond.
6
CH2OH
O 1 O
5
H H HOH2C H
H
4 1 2 5
OH H O H HO
HO 3 2 3 4 CH2OH
6
Glycosidic
linkage H
H OH OH
α-D-Glucose Sucrose β-D-Fructose
Q. 4. Amino acids behave like salts rather than simple amines or carboxylic acids. Explain.
[NCERT Exemplar]
Ans. In aqueous solution, the carboxyl group loses a proton and amino group accepts a proton to form a zwitter
ion.
O O
|| ||
R—CH—C—OH R—CH—C—O –
| |
NH 2 NH3
+
(Zwitter ion)
H OH
α-D-(+)-Glucopyranose
H OH
α-D-(+)-Glucopyranose
Biomolecules 583
(iii) Glucose reduces Tollens’ reagent to metallic silver.
CHO COO –
| |
+
(CH—OH) 4 + 2 [Ag (NH3) 2] + 3OH – (CHOH) 4 + 2Ag . + 2H 2 O
| Tollens’s reagent | Silver mirror
CH 2 OH CH 2 —OH
D - (+) - Glu cos e Gluconic acid
l Glycosidic linkage.
+
(ii) a-Amino acids act as zwitter ions, (H3N—CHR—COO–) or dipolar ions. Due to this dipolar salt-like
structure, they have strong dipole-dipole interactions. Therefore, their melting points are higher than
the corresponding halo acids which do not exist as zwitter ions.
Q. 5. (i) Draw the pyranose structure of glucose.
(ii) What type of linkage is present in proteins?
(iii) Give one example each for water-soluble vitamins and fat-soluble vitamins. [CBSE (F) 2016]
6 CH2OH 6 CH2OH
5
O 5
O
H H H H H OH
Ans. (i) 4 1 4 1
OH H OH H
HO 3 OH HO 3 H
2 2
H OH H OH
α-D-(+) Glucopyranose β-D-(+) Glucopyranose
O
||
(ii) Peptide linkage (—C—NH—)
(iii) Vitamin C and B group vitamins are water soluble vitamins.
Vitamins A, D, E and K are fat soluble vitamins.
Q. 6. (i) Write the product obtained when D-glucose reacts with H2N—OH.
(ii) Amino acids show amphoteric behaviour. Why?
(iii) Why cannot vitamin C be stored in our body? [CBSE Patna 2015]
(ii) In aqueous solution, amino acids exist as a zwitter ion. In zwitter ionic form, amino acids show
amphoteric behaviour as they react both with acids and bases.
+ OH – + OH –
—
H3 N CH—COOH +
H3 N—CH—COO – +
H 2 N—CH—COO –
| H | H |
R R R
(I ) Zwitter ion (II)
–
In acidic+medium COO ion of the zwitter ion accepts a proton to form the cation (I) while in basic
medium NH3 loses a proton to form the cation (II).
(iii) As vitamin C is water soluble, therefore, it is readily excreted in urine and hence cannot be stored in
the body.
Self-Assessment Test
Time allowed: 1 hour Max. marks: 30
Choose and write the correct answer for each of the following. (3 × 1 = 3)
1. Which of the following is laevorotatory?
(a) Glucose (b) Sucrose (c) Fructose (d) None of these
2. Amino acids are best represented as:
(a) dipolar ions (b) isoelectric ions (c) amphoteric ions (d) zwitter ions
3. Which one of the following is a peptide hormone?
(a) Testosterone (b) Glucagon (c) Adrenaline (d) Thyroxine
Biomolecules 585
In the following questions, two statements are given—one labeled Assertion (A) and the other labeled
Reason (R). Select the correct answer to these questions from the codes (a), (b), (c) and (d) as given below:
(a) Both Assertion (A) and Reason (R) are correct statements, and Reason (R) is the correct explanation of
the Assertion (A).
(b) Both Assertion (A) and Reason (R) are correct statements, but Reason (R) is not the correct explanation
of the Assertion (A).
(c) Assertion (A) is correct, but Reason (R) is incorrect statement.
(d) Assertion (A) is incorrect, but Reason (R) is correct statement. (3 × 1 = 3)
4. Assertion (A) : The pyrimidine base uracil is present in RNA.
Reason (R) : RNA controls the synthesis of proteins.
5. Assertion (A) : Enzymes are globular proteins.
Reason (R) : Enzymes are regenerated during reactions.
6. Assertion (A) : Maltose is a reducing sugar, one molecule of which gives two molecules of
D-glucose on hydrolysis.
Reason (R) : Maltose has a 1, 4 b-glycosidic linkage.
Answer the following questions:
7. What are anomers? Give one example. (1)
8. What type of protein is present in keratin. [CBSE 2020 (56/4/3)] (1)
9. Which forces are responsible for the stability of a-helix? Why is it named as 3.613 helix? (2)
10. Write the reactions showing the presence of following in the open structure of glucose:
(i) five —OH groups (ii) a carbonyl group [CBSE 2020 (56/4/3)] (2)
11. Define enzymes. How do enzymes differ from ordinary chemical catalysts? (2)
12. What is essentially the difference between a-form of glucose and b-form of glucose?
[CBSE Delhi 2011] (2)
13. The Fischer projection of D-Glucose is given alongside. CHO
(i) Give the Fischer projection of L-Glucose. H OH
HO
(ii) What happens when L-Glucose is treated with Tollens’ reagent? H (2)
H OH
H OH
14. Define the following terms: CH 2OH
(i) Polysaccharides (ii) Amino acids (iii) Enzymes [CBSE (F) 2014] (3)
15. (i) Name the three major classes of carbohydrates and give an example of each of these classes.
(ii) What type of linkage is responsible for the primary structure of proteins?
(iii) Name the location where protein synthesis occurs in our body. (3)
16. (i) Write about the following on protein synthesis:
(a) Name the location where protein synthesis occurs.
(b) How do 64 codons code for only 20 amino acids?
(c) Which of the two bases of the codon are more important for coding? (3)
(ii) What deficiency diseases are caused due to lack of vitamins A, B1, B6 and K in human diet?
17. (i) Comment on the specificity of enzyme action. What is the most important reason for their
specificity?
(ii) (a) What are the products of hydrolysis of maltose?
(b) Name the vitamin whose deficiency causes pernicious anaemia.
[CBSE 2019 (56/2/2)] (3)
Answers
1. (c) 2. (d) 3. (b) 4. (c) 5. (a) 6. (c) zzz