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Proteins and Protein Metabolism 29 CHAPTER 3 PPPROROROTEINSTEINSTEINS ANDANDAND PPPROROROTEINTEINTEIN MMMETETETABOLISMABOLISMABOLISM 1. All proteins contain the (D) All amino acids contain negatively charged (A) Same 20 amino acids side chains (B) Different amino acids 6. pH (isoelectric pH) of alanine is (C) 300 Amino acids occurring in nature (A) 6.02 (B) 6.6 (D) Only a few amino acids (C) 6.8 (D) 7.2 2. Proteins contain 7. Since the pK values for aspartic acid are (A) Only L- α - amino acids 2.0, 3.9 and 10.0, it follows that the (B) Only D-amino acids isoelectric (pH) is (C) DL-Amino acids (A) 3.0 (B) 3.9 (D) Both (A) and (B) (C) 5.9 (D) 6.0 3. The optically inactive amino acid is 8. Sulphur containing amino acid is (A) Glycine (B) Serine (A) Methionine (B) Leucine (C) Threonine (D) Valine (C) Valine (D) Asparagine 4. At neutral pH, a mixture of amino acids 9. An example of sulphur containing amino in solution would be predominantly: acid is (A) Dipolar ions (A) 2-Amino-3-mercaptopropanoic acid (B) Nonpolar molecules (B) 2-Amino-3-methylbutanoic acid (C) Positive and monovalent (C) 2-Amino-3-hydroxypropanoic acid (D) Hydrophobic (D) Amino acetic acid 5. The true statement about solutions of 10. All the following are sulphur containing amino acids at physiological pH is amino acids found in proteins except (A) All amino acids contain both positive and (A) Cysteine (B) Cystine negative charges (C) Methionine (D) Threonine (B) All amino acids contain positively charged 11. An aromatic amino acid is side chains (C) Some amino acids contain only positive (A) Lysine (B) Tyrosine charge (C) Taurine (D) Arginine 28 MCQs IN BIOCHEMISTRY 12. The functions of plasma albumin are 21. An amino acid that does not form an ααα- (A) Osmosis (B) Transport helix is (C) Immunity (D) both (A )and (B) (A) Valine (B) Proline 13. Amino acid with side chain containing (C) Tyrosine (D) Tryptophan basic groups is 22. An amino acid not found in proteins is (A) 2-Amino 5-guanidovaleric acid (A) β-Alanine (B) Proline (B) 2-Pyrrolidine carboxylic acid (C) Lysine (D) Histidine (C) 2-Amino 3-mercaptopropanoic acid 23. In mammalian tissues serine can be a (D) 2-Amino propanoic acid biosynthetic precursor of 14. An example of ααα-amino acid not present (A) Methionine (B) Glycine in proteins but essential in mammalian (C) Tryptophan (D) Phenylalanine metabolism is 24. A vasodilating compound is produced by (A) 3-Amino 3-hydroxypropanoic acid the decarboxylation of the amino acid: (B) 2-Amino 3-hydroxybutanoic acid (A) Arginine (B) Aspartic acid (C) 2-Amino 4-mercaptobutanoic acid (C) Glutamine (D) Histidine (D) 2-Amino 3-mercaptopropanoic acid 25. Biuret reaction is specific for 15. An essential amino acid in man is (A) –CONH-linkages (B) –CSNH2 group (A) Aspartate (B) Tyrosine (C) –(NH)NH2 group (D) All of these (C) Methionine (D) Serine 26. Sakaguchi’s reaction is specific for 16. Non essential amino acids (A) Tyrosine (B) Proline (A) Are not components of tissue proteins (C) Arginine (D) Cysteine (B) May be synthesized in the body from essential amino acids 27. Million-Nasse’s reaction is specific for the amino acid: (C) Have no role in the metabolism (D) May be synthesized in the body in diseased (A) Tryptophan (B) Tyrosine states (C) Phenylalanine (D) Arginine 17. Which one of the following is semi- 28. Ninhydrin with evolution of CO2 forms a essential amino acid for humans? blue complex with (A) Valine (B) Arginine (A) Peptide bond (B) α -Amino acids (C) Lysine (D) Tyrosine (C) Serotonin (D) Histamine 18. An example of polar amino acid is 29. The most of the ultraviolet absorption of proteins above 240 nm is due to their (A) Alanine (B) Leucine content of (C) Arginine (D) Valine (A) Tryptophan (B) Aspartate 19. The amino acid with a nonpolar side chain (C) Glutamate (D) Alanine is 30. Which of the following is a dipeptide? (A) Serine (B) Valine (C) Asparagine (D) Threonine (A) Anserine (B) Glutathione (C) Glucagon (D) -Lipoprotein 20. A ketogenic amino acid is β (A) Valine (B) Cysteine 31. Which of the following is a tripeptide? (C) Leucine (D) Threonine (A) Anserine (B) Oxytocin (C) Glutathione (D) Kallidin PROTEINS AND PROTEIN METABOLISM 29 32. A peptide which acts as potent smooth 43. The amino acid from which synthesis of muscle hypotensive agent is the protein of hair keratin takes place is (A) Glutathione (B) Bradykinin (A) Alanine (B) Methionine (C) Tryocidine (D) Gramicidin-s (C) Proline (D) Hydroxyproline 33. A tripeptide functioning as an important 44. In one molecule of albumin the number reducing agent in the tissues is of amino acids is (A) Bradykinin (B) Kallidin (A) 510 (B) 590 (C) Tyrocidin (D) Glutathione (C) 610 (D) 650 34. An example of metalloprotein is 45. Plasma proteins which contain more than (A) Casein (B) Ceruloplasmin 4% hexosamine are (C) Gelatin (D) Salmine (A) Microglobulins (B) Glycoproteins (C) Mucoproteins (D) Orosomucoids 35. Carbonic anhydrase is an example of 46. After releasing O at the tissues, (A) Lipoprotein (B) Phosphoprotein 2 hemoglobin transports (C) Metalloprotein (D) Chromoprotein (A) CO2 and protons to the lungs 36. An example of chromoprotein is (B) O2 to the lungs (A) Hemoglobin (B) Sturine (C) CO2 and protons to the tissue (C) Nuclein (D) Gliadin (D) Nutrients 37. An example of scleroprotein is 47. Ehlers-Danlos syndrome characterized by (A) Zein (B) Keratin hypermobile joints and skin abnormalities (C) Glutenin (D) Ovoglobulin is due to (A) Abnormality in gene for procollagen 38. Casein, the milk protein is (B) Deficiency of lysyl oxidase (A) Nucleoprotein (B) Chromoprotein (C) Deficiency of prolyl hydroxylase (C) Phosphoprotein (D) Glycoprotein (D) Deficiency of lysyl hydroxylase 39. An example of phosphoprotein present 48. Proteins are soluble in in egg yolk is (A) Anhydrous acetone(B) Aqueous alcohol (A) Ovoalbumin (B) Ovoglobulin (C) Anhydrous alcohol (D) Benzene (C) Ovovitellin (D) Avidin 49. A cereal protein soluble in 70% alcohol 40. A simple protein found in the nucleopro- but insoluble in water or salt solution is teins of the sperm is (A) Glutelin (B) Protamine (A) Prolamine (B) Protamine (C) Albumin (D) Gliadin (C) Glutelin (D) Globulin 50. Many globular proteins are stable in 41. Histones are solution inspite they lack in (A) Identical to protamine (A) Disulphide bonds (B) Hydrogen bonds (B) Proteins rich in lysine and arginine (C) Salt bonds (D) Non polar bonds (C) Proteins with high molecular weight (D) Insoluble in water and very dilute acids 51. The hydrogen bonds between peptide linkages of a protein molecules are inter- 42. The protein present in hair is fered by (A) Keratin (B) Elastin (A) Guanidine (B) Uric acid (C) Myosin (D) Tropocollagen (C) Oxalic acid (D) Salicylic acid 30 MCQs IN BIOCHEMISTRY 52. Globular proteins have completely folded, 60. At the lowest energy level ααα-helix of coiled polypeptide chain and the axial polypeptide chain is stabilised ratio (ratio of length to breadth) is (A) By hydrogen bonds formed between the H of (A) Less than 10 and generally not greater than peptide N and the carbonyl O of the residue 3–4 (B) Disulphide bonds (B) Generally 10 (C) Non polar bonds (C) Greater than 10 and generally 20 (D) Ester bonds (D) Greater than 10 61. Both ααα-helix and βββ-pleated sheet confor- 53. Fibrous proteins have axial ratio mation of proteins were proposed by (A) Less than 10 (A) Watson and Crick (B) Less than 10 and generally not greater than (B) Pauling and Corey 3–4 (C) Waugh and King (C) Generally 10 (D) Y.S.Rao (D) Greater than 10 62. The primary structure of fibroin, the 54. Each turn of α -helix contains the amino principal protein of silk worm fibres acid residues (number): consists almost entirely of (A) 3.6 (B) 3.0 (A) Glycine (B) Aspartate (C) 4.2 (D) 4.5 (C) Keratin (D) Tryptophan 55. Distance traveled per turn of α−α−α−helix in 63. Tertiary structure of a protein describes nm is (A) The order of amino acids (A) 0.53 (B) 0.54 (B) Location of disulphide bonds (C) 0.44 (D) 0.48 (C) Loop regions of proteins (D) The ways of protein folding 56. Along the ααα-helix each amino acid residue advances in nm by 64. In a protein molecule the disulphide bond (A) 0.15 (B) 0.10 is not broken by (C) 0.12 (D) 0.20 (A) Reduction 57. The number of helices present in a (B) Oxidation collagen molecule is (C) Denaturation (A) 1 (B) 2 (D) X-ray diffraction (C) 3 (D) 4 65. The technique for purification of proteins that can be made specific for a given 58. In proteins the ααα-helix and βββ-pleated sheet protein is are examples of (A) Gel filtration chromotography (A) Primary structure (B) Secondary structure (B) Ion exchange chromatography (C) Tertiary structure (D) Quaternary structure (C) Electrophoresis 59. The a-helix of proteins is (D) Affinity chromatography (A) A pleated structure 66. Denaturation of proteins results in (B) Made periodic by disulphide bridges (A) Disruption of primary structure (C) A non-periodic structure (B) Breakdown of peptide bonds (D) Stabilised by hydrogen bonds between NH and CO groups of the main chain (C) Destruction of hydrogen bonds (D) Irreversible changes in the molecule PROTEINS AND PROTEIN METABOLISM 31 67. Ceruloplasmin is 77. A lipoprotein inversely related to the incidence of coronary artherosclerosis is (A) α1-globulin (B) α2-globulin (C) β-globulin (D) None of these (A) VLDL (B) IDL 68.
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