24.

Antibodies are
(a) Carbohydrates (b) Proteins
(c) Lipids (d) Enzymes
15, Those amino acids which 25. The human body does not produce
by animal bodies are cannot be synthesised
called (a) enzymes (b) DNA
(a) non-essential (6) essential (c) vitamins (d) hormones
(c) energy yielding (d) active 26. Riboflavin deficiency causes
(a) Scurvy (b) Pellagra
(c) Beri-Beri (d) Cheilosis
27. Continuous bleeding from an injured part of
is due to deficiency of
(b) Vitarmin-E
body
(a) Vitamin-A
(c) Vitamin-B, (d) Vitamin-K
17. The pH value of the solution in which a 28. Which of the following B group vitamin can h.
amino acid does not migrate under the particular
influence stored in our body ?
of electricfield is called its (b) Vitamin B,
(a) Vitamin B
(a) Eutectic point (b) Isoelectric point (c) Vitamin B (d) Vitamin B
(c) Effusion point (d) Neutralization point 29. Which of the following acids is a vitamin ?
(a) Aspartic acid (b) Ascorbic acid
(c) Adipic acid (d) Saccharic acid
30. Cyanocobaltamine is the chemical name of
(a) Vitamin B, (b) Vitamin B,
(c) Vitamin B, (a) Vitamin B2
31. Vitamin A is
19. a-Hexical structure refers to (a) ascorbic acid (b) retinol
(a) primary structure of proteins (c) calciferol (d) thiamine
(b) secondary structure of proteins 32. Antiserility vitamin is
(c) tertiary structure of proteins (a) vitamin D (b) vitamin B group
(c) vitamin E (d) vitamin A
(a) quaternary structure of proteins
20. a-Helix and B-pleated structures of proteins are 33. The vitamins absorbed from intestine along with
fats are
stabilized by
(a) A, D (b) A, B
(a) peptide bonds (b) van der Waals forces
(c) A, C (d) D, B
(c) hydrogen bonds
(d) dipole-dipole interactions
21. The end point of protein digestion is
(a) peptides (b) peptones
(c) proteones (d) a-amino acids
22. Peptide bonds are key feature of
(a) Polysaccharides (b) Vitamins
(c) Nucleotides (d) Proteins 3
 these amino acids are called essential acias
while others are called non-essential amino
acids. Each a-amino acidis characterised by
its own isoelectric point. Further, proteins are
classified as fibrous and globular proteins. The
Structures of proteins are discussed at four
different levels. Each protein in the biological
II. Proteins System has its own unique three-dimensional
structure and is associated with a specific
25. W
What is the importance of amino acids to biological activity. When a biologically active
us? protein is subjected to change in temperature,
Ans. Theyare the building blocks of ;proteins which pH, etc. It loses its biological activity and such
are essential for the growth and maintenance a protein is called denatured protein.
29. What is a peptide bond ?
(Hr. Board 2011 : CBSE 2011, 2012)
oflife.
26. How do. amino acids form proteins ? Ans. The covalent bond -NH CO- formed
Anc C-Amino acids undergo condensation reaction between -NH, group of one amino acid and
between -NH, group of one acid and -CoOH COOH of the other with elimination of a
group of the other with elimination of H,O molecule of H,0 is called a peptide bond.
molecule. 30. What is isoelectric point ?
27. In what respect would any two naturally Ans. The pH at which there is no net migration of
influence of an applied
occurring amino acids differ from one the amino acid under the
For
another ? electric field is called isoelectric point. 6.1,
example, the isoelectric point of glycine is
Ans. Allthe naturally occurring a-amino acids differ lysine is
from one another inthe nature of the side chain that of aspartic acid is 3-0 and that of
groups R. For example, in alanine, the side 9.7. (Table 14.2, page 14/21)
fibrous protein
chain is CH, group and in phenylalanine it is 31. Give one example each for (CBSE 2016)
and globular protein.
CH,CoHs group. skin, hair, nails
Giveone example.
28. What are zwitterions ? (Assam Ans. () Fibrous protein : Keratinin
Board 2012: and wool.
which
Maharashtra Board 2012: HP Board 2013) (i) Globular protein : Haemoglobin
blood to muscles.
transports oxygen from the
Or Write the zwitterion structure of glycine. happens when protein is denatured ?
amino 32. What
Or Name the species formed when an (CBSE 2010. 2018)
acid is dissolved in water. form is subjected
Ans. When a protein in the native
(CBSE Sample Paper 2019-2020) etc. H-bonds
tochange of temperature, pH,activity of the
formed by
Ans. A zwitterion is a dipolar ionbasic centres are broken and the biological
neutralization of acidic and protein is lost. Such proteins are called
present within the molecule.
sulphanilic denatured proteins. During denaturation, the
For example, all aminoacids and secondary and tertiary structures are destroyed
intact.
acid exist as zwitterions. but primary structure remains is
denaturation
The most common example of
H,N- CH, CO0" HN the coagulation of white of an egg on [Link]
Glycine Sulphanilic acid When soluble globular protein albumin
converted into insoluble fibrous proteins.
and answer the Another example is curdling of milk which is
Read the given passagefollow : caused due to formation of lactic acid (from
questions 29 to 33 that lactose present in milk) by the bacteria present
essential for growth
raragraph 2. Proteins are beings. These are in milk. Yet another example is the formation
living of cheese from milk when it is heated with an
and maintenance of a-amino acids joined
ade up hundreds of bonds. About 20 a- acid such as lemon juice or tartaricacid. During
together through peptide isolated from the this denaturation, the globular milk protein
amino acids have been proteins. Some of becomes fibrous.
hydrolysis of most of the
 33. Give the
proteins biological
: functions of the following while silk protein fibroin has B-pleated
() Haemoglobin (ii)
structure.
sheet
Collagen 42, What forces are responsible
for
(Karnataka Board 2012)
Ans. (i) Haemoglobin present in blood transports
a-helix?
Ans. -Helix structure is stabilized by
stability of
OXygen from lungs to all the tissues
and CO, from the tissues to the lungs
exhale.
of the body
for
H-bonding between N-H of one
residue and C = ) of the
residue within the polypeptide
intramolecular
fourthchain.-amino acid
amino acid
(ii) Collagen is a fibrous 43. Write one difference between
protein present in a-helix and
connecting tissues of tendons, cartilages and B-pleated structure of proteins.
bones.
34. Give one example each of
essential and non Ans. In a-helix structure, intramolecular (CBSE 2018
[Link]
essential amino acids. takes place while in
Ans. Essential amino acid valine or B-pleated
intermolecular H-bonding takes place,
phenylalanine
Non-essential amino acid-glycine or alanine.
44. Name the central metal atom
present in
35. What are the ultimate products of digestion haemoglobin and chlorophyll.
of proteins ? Ans. Haemoglobin (Fe) and chlorophyll (Mg).
Ans. -Amino acids. 45. Differentiate between keratin and insulin
36. What is a Ans. Keratin is a fibrous protein while insulin is a
prosthetic group ?
Ans. A prosthetic group is a globular protein.
non-protein
obtained by hydrolysis of portion 46. What causes the disease sickle cell
anaemia ?
The main function of the conjugated proteins. Ans. Defective haemoglobin which is produced due
prosthetic group is
control the biological functions of proteins. to to replacement of one amino acid, i.e., glutamic
37. Write the name of the acid by valine.
linkage joining two
amino acids. (CBSE 2013)
Ans. Peptide bond, CO-NH,
38. How many peptide linkages are
present in a
tripeptide ? (CBSE Sample Paper 2018-19)
Ans. A dipeptide contains one peptide bond,
therefore,a tripeptide will contain two peptide
bonds.
39. What is a polypeptide ? Give one example.
Ans. Polypeptides are formed when several
molecules of a-amino acids are joined together
by peptide bonds. For example, oxytocin is a
nanopeptide, i.e., contains 9 a-amino acid units
while insulin contains 51 a-amino acid units.
40. What type of bonding occurs in globular
proteins?
Ans. van der Waals interactions, disulphide bridges,
dipolar interactions (ionic) and hydrogen
bonding.
41. What is the secondary structure of proteins ?
Ans. Conformation which a polypeptide chain
assumes as a resultof H-bonding is called the
secondary structure of protein. There are two
types of secondary structures : -helix and B
pleated sheet structure. For example,a-keratin
in hair, nail, wool, etc. has a-helix structure
 Q. 14.4. The melting points and
corresponding
Ans. The amino
haloacids. solubility
Explain. in water of
amino acias are nigher than those of the
acids exist as +

they have strong

are higher than
Zwitterions,
dipole-dipole
H,
N-CHR--CO0 . Due to this
haloacids attractions or
electrostatic dipolar salt like character
interact strongly with H,[Link] do not have salt attractions.
like character. Therefore, their
As a result, Further, due to salt like melting points
corresponding solubility
Q. 14.5. Where does thehaloacids which do not have salt like
in water of amino acids is character,
higher than they
that of the
Ans. When the egg is water present in the egg go after character.
boiling the egg ?
present inthe eggboiled,
gets
the proteins first
undergo denaturation and then coagulation, and the water
0. 14.6. Why cannot absorbed/adsorbedin the coagulated
vitamin C be stored in our body ? proteins probably through H-bonding.
Ans. Vitamin C is water
soluble, therefore, it is readily excreted in (Kerala Board 2012: Raj. Board 2012)
body. urine and hence cannot be stored in the
 CBSE 2008)
are essential and
Q. 14.11. What non-essential amino acids ? Give two examples of each
type.
(Hr. Board
2012, 2013 ; CBSE 2010, 2018)
Ans d-Amino acids which are needed for health and
growth of human beings but are not synthesized by the
human body are called essential amino acids. For example, valine, leucine,
phenylalanine, etc. On the
other hand, -amino acids which are needed for health and growth of human beings and are synthesized
by the human body are called non-essential amino acids. For example, glycine, alanine, aspartic acid,
etc.
 Q. 14.12. Define the following as related toproteins.
(i) Peptide linkage (CBSE 2011, 2012: Hr. Board 2011, 2012; Assam
(ti) Primnary structure 201 Buard
(iit) Denaturation. (Hr. Board 2012; Assam Board 2013;
CBSE 200% (CBSE. 20L
Ans. () Peptide bond. Proteins are condensation polymers of a-amino acids in which the same or 2018

linkage dfifoerrmenmed
-amino acids are connected by peptide bonds. Chemically, a peptide bond is an amide
between-COOH group of one a- amino acid and -NH, group of the other O- amino acid by
molecule of water. For example, loss ofa

H,N-CH-OH + HHN-ÇH-COOH
-co -H,0 H,N-CH;C NH
Glycine
H,
Alanine Peptide bond
-CCH,H-CO0H
Glycylalanine (Gly-Ala)
(ü) Primary structure. Proteins may contain one or more polypeptide chains. Each
has a large number of -amino acids which are linked to one another in a specific polypeptide chain
sequence. Th.
specific sequence in which the various a-amino acids present in a proteinare linked to one anotheri.
called its primary structure. Any change in the sequence of a-amino acids creates a different Drotein
The general primary structure of a protein is given in Fig. 14.12, page 14/27.
(ii) Denaturation. Each protein in the biological system has a unique three-dimensional structure and
has specific biological activity. This is called native form of a protein. When a protein in its native
form is subjected to physical changes such as change in temperature, p, etc. hydrogen bonds are
broken. Due to cleavage of hydrogen bonds, unfolding of protein molecule occurs and the protein
loses its biological activity. This loss of biological activity is called denaturation. During denaturation,.
2° and 3° structures of proteins are destroyed but 1° structure remains intact (Fig. 14.19,
page 14/31),
As a result of denaturation, globular proteins (soluble in H,0) are converted into
fibrous proteins
(insoluble in H,0).In other words, denaturation leads to coagulation. That is why coagulated proteins
are also called denaturated proteins.
The most common example of denaturation of proteins is the coagulation of albumin present in the
white of an egg. When the egg is boiled hard, the soluble globular protein present in it is denatured and
is converted into insoluble fibrous protein. Another example is curdling of milk which is caused due to
formation of lactic acid by the bacteria present in milk.
Q. 14.13. What are the common types of secondary structure of proteins ?
Ans. The conformation which the polypeptide chains assume as a result of hydrogen bonding is calleu
the secondary structure of the proteins. The two types of secondary structures are : &- helix (Fy
14.14b, page 14/28) and B-pleated sheet structure (Fig. 14.15, page 14/29). Refer to the text re
further details.
Q. 14.14. What type of bonding helps in stabilising the a-helix structure of proteins ?
(CBSE 2010 S, 2013
Ans. The a-helix structure of proteins is stabilized by intramolecular H-bonding between C=00
amino acid residue and the N--H of the fourth aminoacid residue in the chain. Refer to Fig. I*:
Page 14W28.
 S)
Q. 14.15.
Differentiate between globular and fbrous proteins. (Hr. Board 2012 ; CBSE 2010. 2010
Ans. The main differences in globular and fibrous proteins are given in the following table.
Globular proteins Fibrous protefns
1. Globular proteins have almost spheroidal 1. Polype ptide chains of fibrous proteins consist
which tend to lie side
shape due to folding of the polypeptide chain. of thread like molecules
by side to form fibres.
2. Globular proteins are soluble in water. 2. Fibrous proteins are insoluble in water.
3. Globular proteins are sensitive to small3. Fibrous proteins are stable to moderate changes
changes of temperature and pH. Therefore, of temperature and pH.
they undergo denaturation on heating or on
treatment with acids/bases.
4. Globular proteins possess biological activity. 4. Fibrous proteins do not have any biological
That is why they act as enzymes, (maltase, activity but serve as chief structural material
invertase, etc.), hormones (insulin) of animal tissues. For example, keratin in skin,
antibodies (gamma globulins), transport hair, nails, and wool ; collagen in tendons,
agents (haemoglobin), etc. fibroin in silk and myosin in muscles.
(CBSE 2018)
Q. 14.16. How do you explain the amphotericbehaviour of amino acids ?
Ans. Amino acids contain an acidic (carboxyl group) and a basic (amino) group within the same molecule.
In aqueous solution, they neutralize each other. The carboxyl group loses a proton while the amino
group accepts it. As a result, a dipolar or zwitterion is formed.
+

H,N-ÇHCOOH H,N-ÇH-COO
R R

Zwitterion
In zwitterionic form, a-amino acids show amphoteric behaviour as they react with both acids and
bases.
In the acidic medium, CO0 ion of the zwitterion accepts a proton to form the cation (I) while in the
basic medium, NH, ion loses a proton to form the anion (II).
+
OH + OH
H, N CH-COOH
H*
H, N-CH-CO0 H,N-CH-CO0 OOK
Ht
R R R
(I) Zwitterion
+ (u)
Thus, NH, group acts as the acid while CO0 group acts as the base.
 Q. 14.18. 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 ard 2012
As a result of denaturation, the globular proteins (soluble in H,0) are converted into
remains
intact.
fibrous proteins
(insoluble in H,0) and their biological activity is lost. For example, boiled egg which contains,
ains coagulate
proteins cannot be hatched to produce chickens.
Q. 14.19. How are vitamins classified 2 Name the vitamin responsible for coagulation of blood ?
Ans. Vitamins are classified into two groups depending upon their solubility in water or fat.
() Water soluble vitamins. These include vitamin B-complex(B, B, B4, i.e., nicotinic
pantothenic acid, B. B, and folic acid) and vitamin C. acid, [Link],
(ii) Fat soluble vitamins. These
These include vitamins A, D, Eand K. They are stored in liver
liver and adiposeose
(fat storing tissues).
However, biotin, i.e.,vitamin His neither soluble in water nor infat.
Vitamin Kisresponsible for coagulation of blood.
Q. 14.20. Why are vitamin A and vitamin C essential to us ? Give their important
Ans. Vitamin A is essential to us because its deficiency causes xerophthalmia (hardening of cornea of eve
and night blindness.
Sources : Fish liver oil, carrots, butter and milk.
Vitamin C. Vitamin C is essential to us because its deficiency causes scurvy (bleeding gums) and
Pyorrhea (loosening and bleeding of teeth).
Sources : Citrous fruits ; amla, green leafy vegetables.