CHEMISTRY MCQs (PART 4)
CHEMISTRY MCQs (PART 4)
128. Physiologically active configuration of amino acids:
(A) L
(B) D
(C) For some amino acids it is either of two
(D) Neither L nor D
129. Cystine is synthesized from
(A) Cysteine
(B) Methionine
(C) Arginine
(D)
Leucine
130. The major constituent of the proteins of hair and keratin of skin:
(A) Arginine
(B) Cysteine
(C) Glycine
(D) Arginine
131. NH3 is removed from
brain mainly by
(A) Creatinine formation
(B) Uric acid production
(C) Urea
formation
(D) Glutamine formation
132. Mechanism by which NH3 is removed from
the kidneys is
(A) Urea formation
(B) Uric acid formation
(C) Creatinine
formation
(D) None of these
133. Low density plasma proteins are rich in
(A)
Chylomicrons
(B) Cholesterol
(C) Triglycerides
(D) Phospholipids
134.
Transcortins are
(A) Mucoproteins
(B) Glycoproteins
(C) Metalloproteins
(D)
Lipoproteins
135. Proteins that carries Iron into different tissues is
(A)
Ceruloplasmin
(B) Trans cortin
(C) Mucoproteins
(D) Glycoproteins
136.
Naturally occurring amino acids have
(A) L-Configuration
(B) D-Configuration
(C) DL-Configuration
(D) None of these
137. Abnormal chain of aminoacids in
sickle cell anemia is
(A) β-chain
(B) β-chain
(C) γ-chain
(D) r-chain
138. A dietary deficiency of tryptophan and nicotinate leads
to
(A) Beri Beri
(B) Xerophthalmia
(C) Anemia
(D) Pellegra
139. Which one of
the following is an essential amino acid?
(A) Arginine
(B) Tyrosine
(C)
Phenylalanine
(D) Proline
140. One of the following amino acid is solely
ketogenic:
(A) Lysine
(B) Alanine
(C) Valine
(D) Glutamate
141. Along with CO2,
NH3 and ATP, the amino acid that is needed in urea cycle is
(A) Alanine
(B)
Isoleucine
(C) Aspartate
(D) Glycine
142. Isoelectric pH of an amino acid is
that pH at which it has a
(A) Positive charge
(B) Negative charge
(C) No charge
(D) None of these
143. Which of the following contributes nitrogen atoms to
both purine and pyrimidine rings?
(A) Aspartate
(B) Carbamoyl phosphate
(C) CO2
(D) Glutamine
144. Which amino acid is a lipotropic factor?
(A) Lysine
(B)
Lecuine
(C) Tryptophan
(D) Methionine
145. Which of the following protein is
rich in cysteine?
(A) Elastine
(B) Collagen
(C) Fibrin
(D) Keratin
146. Which
amino acid is present at 6th position of β-chain of Hbs instead of glutamate in
HbA?
(A) Cysteine
(B) Valine
(C) Aspartate
(D) Glutamate
147. The amino acid
which contains an indole group is
(A) Histidine
(B) Arginine
(C) Cystine
(D)
Tryptophan
148. From two amino acids peptide bond formation involves removal of
one molecule of
(A) Water
(B) Ammonia
(C) Carbondioxide
(D) Carboxylic acid
149. Polymers of more than 100 amino acids are termed
(A) Proteins
(B)
Polypeptides
(C) Both (A) and (B)
(D) None of these
150. The example of
globulins:
(A) Leucosin
(B) Tuberin
(C) Oryzenin
(D) Legunelin
151. The example
of scleroproteins:
(A) Glutamin
(B) Giladin
(C) Salmine
(D) Elastin
152. The
example of phosphoprotein:
(A) Mucin
(B) Ovovitellin
(C) Ovomucoid
(D)
Tendomucoid
153. The example of metalloproteins:
(A) Siderophilin
(B) OREES
mucoid
(C) Elastin
(D) All of these
154. The example of chromoprotein:
(A)
Salmine
(B) Catalase
(C) Zein
(D) Gliadin
155. Deamination is ______ of amino
group.
(A) Removal
(B) Addition
(C) Supplementation
(D) None of these
156.
Proteins produce polypeptides from proteins by
(A) Oxidizing
(B) Reducing
(C)
Hydrolyzing
(D) None of these
157. Proteins react with biuret reagent which is
suggestive of 2 or more
(A) Hydrogen bonds
(B) Peptide bonds
(C) Disulphide
bonds
(D) Hydrophobic bonds
158. The disulphide bond is not broken under the usual
conditions of
(A) Filtration
(B) Reduction
(C) Oxidation
(D) Denaturation
159.
Insulin is oxidized to separate the protein molecule into its constituent
polypeptide chains without affecting the other part of the molecule by the use
of
(A) Performic acid
(B) Oxalic acid
(C) Citric acid
(D) Malic acid
160. Each
hydrogen bond is quite
(A) Weak
(B) Strong
(C) Both (A) and (B)
(D) None of
these
161. A coiled structure in which peptide bonds are folded in regular
manner by
(A) Globular proteins
(B) Fibrous proteins
(C) Both (A) and (B)
(D)
None of these
162. In many proteins the hydrogen bonding produces a regular
coiled arrangement called
(A) α-helix
(B) β-helix
(C) Both (A) and (B)
(D) None
of these
163. Many globular proteins are stable in solution although they lack
in
(A) Hydrogen bonds
(B) Salt bonds
(C) Non-polar bonds
(D) Disulphide bonds
164. Each turn of α-helix contains the number of amino acids
(A) 2.8
(B) 3.2
(C) 3.4
(D) 3.6
65. The distance travelled per turn of α-helix in nm is
(A)
0.34
(B) 0.44
(C) 0.54
(D) 0.64
166. α-helix is disrupted by certain amino
acids like
(A) Proline
(B) Arginine
(C) Histidine
(D) Lysine
167. α-helix is
stabilized by
(A) Hydrogen bonds
(B) Disulphide bonds
(C) Salt bonds
(D)
Non-polar bonds
168. Foetal haemoglobin contains
(A) Two α and two γ chains
(B)
Two β and two γ chains
(C) Both (A) and (B)
(D) None of these
169. When
haemoglobin takes up oxygen there is a change in the structure due to the
moving closer together of
(A) β-chains
(B) β-chains
(C) γ-chains
(D) α and γ
chains
170. The hydrogen bonds in the secondary and tertiary structure of proteins
are directly attacked by (A) Salts
(B) Alkalies
(C) Detergents
(D) All of these
171. The hydrogen bonds between peptide linkages are interfered by
(A)
Guanidine
(B) Uric acid
(C) Salicylic acid
(D) Oxalic acid
172. The
digestability of certain denatured proteins by proteolytic enzymes
(A)
Decreases
(B) Increases
(C) Normal
(D) None of these
173. The antigenic
antibody functions of proteins by denaturation are frequently
(A) Not changed
(B) Changed
(C) Both (A) and (B)
(D) None of these
174. In case of severe
denaturation of protein, there is
(A) Reversible denaturation
(B) Moderate
reversible denaturation
(C) Irreversible denaturation
(D) None of these
175.
When egg albumin is heated till it is coagulated, the secondary and tertiary
structures of the proteins are completely lost resulting in a mixture of
randomly arranged
(A) Dipeptide chains
(B) Tripeptide chains
(C) Polypeptide
chains
(D) All of these
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