Biomolecules PYQS
Biomolecules PYQS
H¢ H
(b) (HOH), (ÇHOH),
H,OH CH,OH
"CH,OH
-D-(+) -Glucose
CH,OH
B-D-(}-Glucose
Glucose cyanohydrin
(c) Refer to answer 26(i).
32. (a) Actually, glucose exists in the cyclic
35. (i) Refer to answer 20.
hemiacetal form with only a small amount
(< 0.05%) of the open chain form. Since, the (iü) Refer to answer 19.
concentration of the open chain form is low and (iii) Refer to answer 25().
its reaction with 2,4-DNP is reversible, therefore, 36. Refer to answers 31 and 24.
formation of 2,4-DNP derivative cannot disturb
37. The sugars which reduce Fehling's solution
the equilibrium to regenerate more of the open and Tollens' reagent are called reducing sugars.
chain form from the cyclic hemiacetal form and
For example, all monosaccharides containing free
hence, does not give this test.
(b) The two strands in DNA molecule are held -CHO Or -=0group are reducing sugars.
together by the hydrogen bonds between purine 38. (c) Peptide linkage is present in proteins.
base of one strand and pyrimidine base of the
other and vice versa. Because of different sizes and 39. Characteristic diferences between globular
geometries of the bases, the only possible pairing and fibrous proteins can be given as :
in DNA are G(guanine) and C(cytosine) through S. Globular proteins Fibrous proteins
three H-bonds, i.e., (C G) and between A No.
(adenine) and T (thymine) through two H-bonds 1.These are cross- These are linear
(i.e, A = T) . Due to this base-pairing principle, linked proteins and condensation
are condensation polymer.
the sequence of bases in one strand automatically
product of acidic
fixes the sequence of bases in the other strand. and basic amino
Thus, the two strands are complementary and not acids.
identical. 2 These are soluble in These are insoluble
(c) The basic structural difference between water, mineral acids in water butsoluble
starch and cellulose is of linkage between the and bases. in strong acids and
bases.
glucose units. In starch, there is c-D-glycosidic
3. These proteins haveThese are linear
three dimensionalpolymers held
folded structure.together by
R R
These are stabilised intermolecular Peptide linkage
by internal hydrogen bonds, 48. An egg contains a soluble globular protein
hydrogen bonding. e.g, hair, silk. called albumin which is present in the white
eg-s cgg albumin,
enzymes. part. On boiling, denaturation (loss of biological
activity) of this protein takes place which results
40. Globular protein - Insulin in the formation of insoluble fibrous proteins. The
Fibrous protein - Keratin water molecules are utilized in this process.
41. As amino acids have both acidic (carboxyl 49. (i) Refer to answer 45.
group) and basic groups (amino group) in the (ii) Refer to answer 44.
same molecule, they react with both acids and 50. (a) Refer to answer 41.
bases. Hence, they show amphoteric behaviour. (b) In -helix structure, intramolecular H-bonding
42. Acidic amino acids are those which contain takes place whereas in B-pleated structure, inter
more number of carboxyl groups as compared molecular H-bonding takes place.
to amino groups whereas basic anmino acids are 51. Primary structure : The specific sequence in
those which contains more number of amino which the various amino acids present in aprotein
groups than carboxyl groups. are linked to one another is called its primary
43. Peptide linkage. structure. Any change in the primary structur
44. Essential amino acids : Amino acids which creates a different protein.
Secondary structure: The conformation
cannot be synthesized in the body and must be
the polypeptide chain is known as secondary
obtained through diet are known as essential structure. The two types of secondary structure
amino acids, e.g., valine, leucine, etc. are o-helix and B-pleated sheet structure.
45. Denaturation : The loss of biological activity In a-helix structure, the polypeptide chain forms
of a protein by changing the pH, temperature all the possible hydrogen bonds by twisting into a
or by adding some salt due to disruption of the right handed screw (helix) with the -NH groups
native structure of protein is called denaturation. of each amino acid residue hydrogen bonded to
During denaturation, secondary and tertiary the C=0 group of an adjacent turn of the helix.
structure of protein is destroyed but primary In B-pleated sheet structure, all peptide chains are
structure remains intact.
stretched out to nearly maximum extension and
46. Organic compounds containing both amino then laid side by side which are held together by
(-NH) and carboxyl (COOH) functional intermolecular hydrogen bonds.
groups are called amino acids. 52. Refer to answer 47.
R-CH-COOH 53. (i) Amylose is a linear condensation polymer
of a-D-glucose in which C, of one glucose unit is
47. Proteins are the polymers of a-amino acids attached to C, of the other through a-glycosidic
linked by amide formation between carboxyl and linkage while amylopectin is a highly branched
amino group. This is called peptide linkage or polymer in which C, of terminal glucose unit in
peptide bond, e.g. each chain is further linked to Cof some other
glucose unit in the next chain through C,-C growth and health of the organism are called
-glycosidic linkage. vitamins.
(i) Peptide linkage is an amide linkage formed 66. The deficiency of vitamin A leads to
between -COOH group of one d-amino acid and xerophthalmia and night blindness. The deficiency
-NH, group of the other amino acid by loss of a of vitamin C leads to scurvy.
molecule of water whereas a linkage between two 67. Vitamin - A: Night blindness
monosaccharides units through oxygen atom is Vitamin E: Muscular weakness.
called glycosidic linkage. 68. Vitamin C is water soluble and powerful
(iii) Refer to answer 39. antioxidant. Natural source of vitamin C is amla.
54. (i) Refer to answer 47. 69. Vitamin D
(ii) Refer to answer 51.
Disease caused due to deficiency of Vitamin D is
(i) Refer to answer 45. rickets.
55. Amino acids which cannot be synthesised 70.
in the body and must be obtained through diet Hormones Vitamins
are known as essential amino acids, e.g, valine (i) The biomolecules These are essential
and leucine. There are ten essential amino acids. which transfer dietary factors
Amino acids which can be synthesised in the information from one required by an
body are known as non-essential amino acids, e.g, group of cell to distant organism in minute
alanine and glutamic acids. tissue or organ. quantities.
56. (a) Refer to answer 39. |() They are produced in They are supplied to
the body in ductless|the body from thel
(b) Protein is denatured and its biological activity glands. food eaten.
Slost.
71. Refer to answer 67.
57. Most of the chemical reactions which occur 72. Vitamin B
in living systems process at very slow rates under 73. Vitamins are classified into two groups
mild condition of temperature and pH. These
reactions are catalysed by a group of biomolecules depending upon their solubility in water or fat.
called enzymes. () Fat soluble vitamins, (e.g, vitamin Aand D)
58. Substances which catalyse chemical
(ii) Water soluble vitamins, (e.g, vitamin B and
C) vitamin K is responsible for the coagulation of
reactions taking place in living organisms are blood.
called biocatalysts, e.g., enzymes.
74. Nucleoside contains pentose sugar, and base
59. Vitamin C is soluble in water and regularly whereas nucleotide contains pentose sugar, base
excreted in urine and hence cannot be stored in
as well as phosphate group.
body. Nucleoside = Base + Sugar
60. Vitamin D Nucleotide - Base + Sugar + Phosphate
61. Vitamin C 75. Ester linkage
62. Vitamin A 76. Uracil
63. Vitamin D 77. Refer to answer 74.
64. Vitamin C 78. DNA is reserve of genetic information and
65. Organic compounds required in the diet responsible for heredityy transmission.
in small amounts to perform specific biological 79. Structural ditferences between DNA and
functions for normal maintenance of optimum RNA
(i) The sugar in DNA is deoxyribose while that 82. Refer to answer 79.
in RNA is ribose. Common bases in DNA and RNA are adenine,
(ii) DNA has a double-stranded helical structure, guanine and cytosine.
while RNA has a single-stranded helical structure. 83. RNA are of three types :
Functional differences between DNA and RNA (i) Messenger RNA (m-RNA): Function as
(i) DNA is the chemical basis of heredity and messenger carrying the information in a gene to
is responsible for maintaining the identity of the protein synthesizing machinery.
ditferent species. (i) Transfer RNA (-RNA) : They transfer the
(i) RNA molecules are responsible for protein amino acids from cytoplasm to the protein
synthesis but the message for the synthesis of a synthesizing machinery.
particular protein is present in DNA. (iii) Ribosomal RNA (r-RNA) : They associates
with a set of proteins to form ribosomes. These
80. Refer to answer 79. complex structures, which physically move among
In DNA, thymine is present. an m-RNA molecule, catalyze the assembly of
81. The bases present in RNA are adenine (A), amino acids into protein chains. They also bind
guanine (G) cytosine (C) and Uracil (U). t-RNAs and various molecules necessary for
Uracil is not present in DNA. protein synthesis.