Chapter - 9 Biomolecule DPP - 1 PDF
Chapter - 9 Biomolecule DPP - 1 PDF
Chapter - 9 Biomolecule DPP - 1 PDF
C) H & N D) N & O
Biomolecules 5. For the chemical composition
analysis____ is used:-
1. Elemental analysis on a plant tissue,
A) CH3COOH B) CH3COOH – Cl
Animal tissue or a microbial paste
C) Cl3 – CCOOH D) Cl3 – COOH
reveals:-
6. Filtrate obtained after grinding of
A) list of elements like C; H; O &
living tissue is also known as:-
several others
A) Slurry B) Acid - soluble
B) Respective content per unit mass
C) Acid insoluble pool
of a living tissue
D) All
C) Both
7. Acid – insoluble pool is also known
D) Diversity of living organism in our
as:-
Biosphere.
A)Slurry B) Retentate
2. Elemental analysis on earth’s crust
C) filtrate D) All
reveals:-
8. Analytical techniques applied to the
A) list of elements like C; H; O &
compound gives us an idea of:-
several others
A) Atomic formula
B) Respective content per unit mass
B) Molecular formula of compounds.
of a living tissue
C) Both
C) Both
D) None
D) Diversity of living organism in our
9. All the carbon compounds that we get
Biosphere.
from the living tissue can be called:-
3. Elemental list could be _____ in _____
A) Biomolecules B) Slurry
terms of study on living tissues &
C) Retentate D) All
earth’s crust:-
10. If the tissue is fully burnt:-
A) Same; absolute
A) All the carbon compounds are
B) Different; absolute
oxidised to gaseous forms (CO2 &
C) Different; same
water vapour).
D) Same; relative
B) Remaining’s are known as ash.
C) Ash contains inorganic elements &
Paragraph – 9.1
inorganic compounds.
composition?
ii)
A) Ribose B) Glucose
C) Both D) None iii) Guanine iv) Uracil
41. CH3 – (CH2)14 – COOH
A) A glycerol molecule A) All four B) Only three
B) A fatty acid C) Only two D) Only one
C) An amino acid 45. which of the following group
D) A carbohydrate represents Lectins
42. Which of the following is the A) Abrin; Ricin
compound represents the shown B) Monoterpenes; Diterpenes
figure :- C) Concanavalin – A
D) None of the above
Paragraph – 9.3 iii) Molecular weight do not exceed
800 Da.
A) 1 B) 2
C) 3 D) 4
91. At each of ascent, the strand turn ___ changed into some other
92. One full turn of helix strand of D) Biomolecules are constantly being
Paragraph – 9.12.3
Nature of enzyme action
129. Which is correct way to
represent enzyme action
A) E + S ES ⇌ EP ⇌ E + P
B) E + S ⇌ E + P
C) E + S ⇌ ES EP E + P
D) E + S ES EP ⇌ E +P
(i) (ii) (iii) 130. ES complex is _____ and
A) Activation Transition Activation dissociates into _____ and _____
energy state energy A) Long lived; product; changed
without with enzyme
enzyme enzyme B) Short lived; reaction, changed
B) Transition Activation Activation enzyme
state energy energy C) Long lived, reactant, unchanged
without with enzyme
enzyme enzyme D) Short lived, product, unchanged
C) Activation Activation Transition enzyme
energy energy state 131. Arrange in correct sequence of
with without catalytic cycle of an enzyme action-
enzyme enzyme i) The active site of the enzyme, now
D) Activation Activation Transition in close proximity of the substrate
energy with state breaks the chemical bonds of the
without enzyme substrate and the new enzyme
enzyme product complex is formed
ii) The substrate binds to the active
127. Choose correct response
site of enzyme, fitting into the
i) Y – axis represent potential
active site
energy
iii) The enzyme release the products of
ii) X – axis represent substrate
the reaction and the free enzyme is
iii) Y – axis represent progress of
ready to bind to another molecule
reaction
of the substrate
iv) X – axis represent state
iv) The binding of the substrate
through transition state
induces the enzyme to alter its
A) i) & ii) B) iii) & iv) shape, fitting more tightly around
the substrate.
C) i) & iv) C) ii) & iii A) i ii iii iv
B) i iii ii iv
128. If ‘P’ (product) is at lower level
C) ii iv i iii
than ‘s’ (substrate), the reaction is
D) ii iv i iii
_______
A) Endothermic reaction
B) Exothermic reaction
C) Spontaneous reaction
D) A & C both
Paragraph – 9.12.4 136. As pH increase, enzyme
activity-
A) Constantly increase
Factors affecting enzyme
B) Constantly decrease
activity C) No effect
D) Increase until optimum and
132. Which of the following can decrease further pH
change enzyme activities? 137. With increase in substrate
A) All such activities that can alter concentration, the velocity of the
the tertiary structure of the protein enzymatic reaction –
B) Temperature pH A) Constantly increase
C) Substrate conditions B) Rise at first until Vmax and
D) All of these further no rise
133. Enzyme activity decline- C) No effect
A) Above the optimum value D) Decrease first until Vmax and
B) Below the optimum value increase further
C) A & B both 138. After reaching Vmax, the
D) Enzyme activity never decline enzymatic reaction does not exceed by
134. Optimum pH refer to – any further rise in concentration of
A) pH at which enzyme activity is substrate because-
lowest A) Enzymes molecules are fewer than
B) pH at which enzyme activity is substrate molecules
highest B) After saturation of those enzyme
C) pH at which enzyme activity molecules these are no free
started immediately enzyme molecules to bind with
D) pH at which enzyme activity ended additional substrate molecules
completely C) A & B
135. choose response with respect to D) After saturation of those enzyme
enzyme activities molecules, enzyme get changed it’s
i) low temperature destroy form.
enzyme 139. When the binding chemical
ii) high temperature preserve shut off enzyme activity, the process
enzyme in a temporarily is called ______ and the chemical is
inactive state called_____
iii) optimum temperature is A) Inhibition; inhibitor
temperature at which enzyme B) Inhibition; cofactors
activity is highest C) Exhibition, exhibitor
iv) As temperature increase, D) None of these
enzyme activity increase until 140. Da what effect is observe on
optimum and thereafter enzyme activity due to inhibitor
increase in temperature lead to A) It fasten enzyme kinetics
decline in enzyme activities B) It decline enzyme kinetics
v) As temperature increase C) It shut off enzyme kinetics
enzyme activities is zero until D) No effect on enzyme kinetics
optimum temperature &
thereafter increase in
temperature lead to increase in
enzyme activities
A) i, iii, iv B) ii, v
C) i, iv, v D) iii, iv
141. Inhibition of succinic i) Hydrolysis of ester, ether, peptide,
dehydrogenase by malonate is due to glycosidic,
A) Malonate is closely resembles with ii) C – C breakdown
substrate succinate in structure iii) C – halide breakdown
B) Malonate is competitive inhibitor iv) P – N breakdown
C) It binds with active site of succinic A) (i) only
dehydrogenase in place of B) (i) & (ii) only
structure C) (iii) & (iv) only D)
D) All of these D) i, ii, iii & iv
142. Competitive inhibitors are often 149. Lysase catalyse _ _ _ _ _ _ of
used in the control of – groups from substrates by mechanism
A) Viral pathogen other than hydrolysis leaving _ _ _
B) Bacterial pathogen bond.
C) Both A & B A. Addition ; double
D) None of these B. Removal ; double
C. Addition ; single
Paragraph – 9.12.5 D. Removal ; triple
150. Isomeric catalyse inter-
Classification & conversion of:
A. Optical isomer
nomenclature of enzyme B. Geometrical isomer
C. Position isomer
143. Enzyme are divided into how
D. All of these
many classes-
151. Linking of two compound is
A) 2 B) 4
achived by-
C) 6 D) 8
A. Lyases
144. Each classes of enzyme were
B. Transferase
further classification into______
C. Ligases
subclass and narned by ___ digit
D. Hydrolase
A) 13; 4 – 13 B) 4 – 13; 13
152. Ligase catalyse-
C) 4 – 13; 4 D) 4; 4 – 13
A. Joining of C-O
145. S reduced + S’ oxidised S
B. Oxidation – reduction of substrate
oxidised + S’ reduced
C. Hydrolysis of C-C
A) Oxidoreductase
D. Conversion of optical isomer
B) Dehydrogenase
C) Transferase
D) A & B both
Paragraph-9.12.6
146. Enzyme catalysing a transfer of
a group i.e. hydrogen between pair of
Co-factors:
substrate S and S’ is-
153. Cofactors are:-
A) Transferase B) Oxidoreductase
A. Proteinous part of enzyme
C) Lyases D) Ligases
B. Non-proteinous part of enzyme
147. Transferases enzyme catalyse a
C. Bound to substrate
transfer of G between pair substrate S
D. Bound to enzyme to make enzyme
& S’.
catalytically retard
G is other than –
A) Oxygen B) Amino
C) Hydrogen D) Carbon
148. Hydrolases catalyse –
154. How many kind of cofactors 160. Choose correct response from
may be identified- following with respect to
A. 1 carboxypeptidase.
B. 2 A. Zine are found as apoenzyme
C. 3 B. It is proteolytic enzyme
D. Zero C. Cofactor are covalent bond with
155. Cofactors are _ _ _ _ _ _ and side chain at active site
apoenzyme are _ _ _ _ part of enzyme. D. Between cofactor and substrate
A. Protein ; protein ionic bond is formed
B. Non-protein ; non-protein 161. How many coordination found
C. Protein ; non-protein in activity of carboxypeptidase?
D. Non-protein ; protein A. Only one ; between cofactor and
156. Prosthetic group are _ _ _ _ _ side chain at active site
and are distinguished from other B. Two between cofactor and side
cofactors in that they are _ _ _ _ _ chain at active site and at to many
bound to apoenzyme. ; same time form one or more bond
A. Organic compound ; tightly with substrate.
B. Organic compound ; loosely C. Zero
C. Inorganic compound ; loosely D. Only one ; between cofactor &
D. Inorganic compound ; tightly substrate
157. Which of following is/are 162. Find mismatch.
correct? Column-I Column-
(i) Haem is prothetic group. II
(ii) Haem is apoenzyme. (a) Carboxypeptid (i) Zine
(iii) Haem is not part of active site of ase
peroxidase. (b) NADP (ii) Niacin
(iv) Haem catalyse the formation of (c) Haem (iii) Peroxida
hydrogen peroxide from water & se
oxygen. (d) NAD (iv) Zine
(v) Haem is part of active site of 163. When cofactor is removed from
peroxidase. enzyme ; what effect is observed.
(vi) Haem catalyse the breakdown of A. Catalytic activity lost
hydrogen peroxide into water & B. Catalytic activity enhance
oxygen. C. Catalytic activity fix at optimum
A. i , iii , vi D. None of these
B. ii , iv , v
C. i , v , vi
D. ii , v , vi
158. NAD & NADP contain-
A. Vitamin niacin
B. Vitamin C
C. Vitamin D
D. Vitamin K
159. Full form of NAD is:-
A. Nicotinamide adenine nucleotide
B. Nicotinamide adenine dinucleoside
C. Nicotinamide adenine dinucleotide
D. Nicotinamide adenine nucleoside
Answer Key: 38. D 76. D 118. D
39. D 77. B 119. A
1. C 120. A
40. A 78. C
2. A 121. C
41. B 79. C 122. D
3. A
42. A 80. D 123. C
4. B 124. C
43. B 81. D
5. C 125. D
44. B 82. C 126. C
6. B
45. C 83. A 127. C
7. B 128. B
46. D 84. D
8. B 129. C
47. B 85. B 130. D
9. A
48. D 86. C 131. D
10. D 132. D
49. B 87. A
11. D 133. C
50. 88. B 134. B
12. C
51. A 89. C 135. B
13. D 136. D
52. A 90. A
14. D 137. B
53. D 91. B
15. D 138. C
54. B 92. B 139. A
16. C
55. D 93. B 140. C
17. A 141. D
56. C 94. B
18. D 142. B
57. C 95. D 143. C
19. A
58. D 96. A 144. B
20. A 145. D
59. A 97. B
21. B 146. B
60. D 98. C 147. C
22. A
61. B 99. C 148. D
23. B 149. B
62. B 100. C
24. B 150. D
63. D 101. A
25. B 151. C
64. C 102. B
152. A
26. D 103. A
65. B 153. B
27. D 104. B
154. C
66. C 105. A
28. A 155. D
67. A 106. D
156. A
29. B 107. C
68. B 157. C
30. A 108. D
158. A
69. B 109. B
31. D 159. C
70. C 110. A
160. B
32. C 111. D
71. D 161. B
33. C 112. B
72. C 162. D
113. D
34. A 163. A
73. C 114. D
35. D 115. C
74. B
36. B 116. B
75. C 117. D
37. C