I. Start the exam by click the “Start” button
PROTEINS AND PROTEIN METABOLISM- Part 19
See all quizzes of PROTEINS AND PROTEIN METABOLISM- Part 19 here:
1 Along with CO2, NH3 and ATP, the amino
acid that is needed in urea cycle is
(A) Alanine (B) Isoleucine
(C) Aspartate (D) Glycine
2. 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
3. Which of the following contributes
nitrogen atoms to both purine and
pyrimidine rings?
(A) Aspartate
(B) Carbamoyl phosphate
(C) CO2
(D) Glutamine
4. Which amino acid is a lipotropic factor?
(A) Lysine (B) Lecuine
(C) Tryptophan (D) Methionine
5. Which of the following protein is rich in
cysteine?
(A) Elastine (B) Collagen
(C) Fibrin (D) Keratin
6. 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
7. The amino acid which contains an indole
group is
(A) Histidine (B) Arginine
(C) Cystine (D) Tryptophan
8. From two amino acids peptide bond
formation involves removal of one
molecule of
(A) Water (B) Ammonia
(C) Carbondioxide (D) Carboxylic acid
9. Polymers of more than 100 amino acids
are termed
(A) Proteins (B) Polypeptides
(C) Both (A) and (B) (D) None of these
10. The example of globulins:
(A) Leucosin (B) Tuberin
(C) Oryzenin (D) Legunelin
11. The example of scleroproteins:
(A) Glutamin (B) Giladin
(C) Salmine (D) Elastin
12. The example of phosphoprotein:
(A) Mucin (B) Ovovitellin
(C) Ovomucoid (D) Tendomucoid
13. The example of metalloproteins:
(A) Siderophilin (B) OREES mucoid
(C) Elastin (D) All of these
14. The example of chromoprotein:
(A) Salmine (B) Catalase
(C) Zein (D) Gliadin
15. Deamination is ______ of amino group.
(A) Removal (B) Addition
(C) Supplementation (D) None of these
16. Proteins produce polypeptides from
proteins by
(A) Oxidizing (B) Reducing
(C) Hydrolyzing (D) None of these
17. Proteins react with biuret reagent which
is suggestive of 2 or more
(A) Hydrogen bonds (B) Peptide bonds
(C) Disulphide bonds (D) Hydrophobic bonds
18. The disulphide bond is not broken under
the usual conditions of
(A) Filtration (B) Reduction
(C) Oxidation (D) Denaturation
19. 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
20. Each hydrogen bond is quite
(A) Weak (B) Strong
(C) Both (A) and (B) (D) None of these
21. 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
22. 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
23. Many globular proteins are stable in
solution although they lack in
(A) Hydrogen bonds (B) Salt bonds
(C) Non-polar bonds (D) Disulphide bonds
24. Each turn of α-helix contains the number
of amino acids
(A) 2.8 (B) 3.2
(C) 3.4 (D) 3.6
25. The distance travelled per turn of α-helix
in nm is
(A) 0.34 (B) 0.44
(C) 0.54 (D) 0.64
26. α-helix is disrupted by certain amino
acids like
(A) Proline (B) Arginine
(C) Histidine (D) Lysine
27. α-helix is stabilized by
(A) Hydrogen bonds (B) Disulphide bonds
(C) Salt bonds (D) Non-polar bonds
28. 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
29. 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
30. 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
