Biochemistry

1st Shifting Exams

I. Classify the Following Amino Acids.

First Column A. Polar uncharged B. Polar Charged C. Nonpolar
Second Column D. Essential E. Nonessential
Third Column F. Aromatic G. Aliphatic

1. Histidine 11. Phenylalanine

2. Glutamic Acid 12. Valine
3. Alanine 13. Threonine
4. Serine 14. Tyrosine
5. Proline 15. Cysteine
6. Arginine 16. Asparagine
7. Methionine 17. Lysine
8. Glutamine 18. Aspartic Acid
9. Leucine 19. Isoleucine
10. Tryptophan 20. Glycine

II. Protein Structures. Choose the letter corresponding to your answer.

21. The bonding present in C 23. The interaction in B

A. Hydrogen Bonding of Side Chain A. Hydrogen Bonding of Side Chain
B. Hydrophobic Interaction B. Hydrophobic Interaction
C. Disulfide Bonding C. Disulfide Bonding
D. Ionic Bonding D. Ionic Bonding
22. Involves Electrostatic Reaction 24. What stabilizes F
A. A A. Hydrogen Bonding
B. E B. Hydrophobic Interactions
C. Both A & E C. Noncovalent Interactions
D. None D. Electrostatic Repulsion
Biochemistry
1st Shifting Exams

25. Capable of Interchain hydrogen bonding C. Both F & G

A. F D. None
B. G
III. Peptides

26. Which of the following is not part of the peptide?

A. Arginine
B. Tyrosine
C. Glycine
D. Alanine
E. Lysine
27. What is the net charge of the peptide
shown above?
A. -1
B. 0
C. +1
D. +2
28. The shown ion form of the peptide is most
likely to be present in which of the
following pH?
A. pH 5
B. pH 10
C. pH 1
D. pH 14
29. What is the isoelectric pH of the peptide?
A. 5.735
B. 6.485 D. 7.125
C. 6.575
30. What is the net charge of the peptide after its final ionizable group is ionized?
A. -1 D. -4
B. -2 E. -5
C. -3
31. Starting at high pH, if the peptide is titrated with an acid, the ionizable group to react first is?
A. Tyrosines -NH3 D. Arginines -NH3
B. Lysines R-NH3 E. Leucines R-COOH
C. Arginines R-NH3
Biochemistry
1st Shifting Exams

32. Which of the following amino-acids is the N-Terminus?

A. E C. C
B. L D. R
33. If the peptide is to fold into a helix the carbonyl group of E will bind to the amino group of ____ via
hydrogen binding?
A. R C. S
B. Y D. E
34. What is the pH of the peptide E-L-L-C-R-Y-S wherein zwitterions exist fully?
A. 6.16 C. 6.49
B. 5.74 D. 6.61

IV. Protein Isolation

Classify the following techniques based on the principle that governs them

A. Based on Size C. Based on Binding Specificity

B. Based on Solubility D. Based on Charge

35. Isoelectric Precipitation 40. Affinity Chromatography

36. Centrifugation 41. Ion Exchange Chromatography
37. Ultrafiltration 42. Dialysis
38. Gel Filtration Chromatography 43. High Performance Liquid
39. Salting-out Chromatography

V. Protein Structures II
A. Collagen C. Both
B. Elastin D. None of the Above

44. Random Coil Conformation 48. Has repeating X-Y-G sequence

45. Desmosome crosslinks 49. Found in connective tissues
46. Triple-Helix Structures 50. Involves hydroxylating enzymes to
47. Fibrous Proteins stabilize the protein
Biochemistry
1st Shifting Exams

A. Hemoglobin C. Both
B. Myoglobin D. None of the Above

51. Tetrahedral arrangement of subunits 54. Thin long and narrow shaped protein
52. Oxygen Storage 55. Tetramer
53. Contains heme

A. Insulin C. Both
B. Glucagon D. None of the Above

56. Secreted by the -cells of pancreas

57. Hypoglycemic Agent
58. Hyperglycemic Agent
59. Maintains homeostasis of glucose
60. Stimulates breakdown of lipids to synthesize glucose
61. Stimulates breakdown of proteins to synthesize glucose
62. Stimulates breakdown of glycogen to synthesize glucose
63. Made up of two polypeptide chains
64. Involves disulfide linkage that are intra and inter chain
65. Endocrine hormones