90 ~ 98 2009/8/18 v.

4
Content

Amino acids, peptide and proteins

Protein structure and function/Heme protein function

Enzyme

Amino acids, peptide and proteins

1. histidine-NH R-group-COOHpKa962
2
pH 5.0(982-2101)
(a) (b) (c) (d)

2. -acid-base catalysisactive site residue

(982-2101)
(a) histidine (b) methionine (c) aspartic acid(d) glutamic
acid

3. (981-2101)
(a) 6 N HCl (b) 8 N NaOH (c) 8 M urea (d) 6 M guanidine HCl

4. aliphatic side chain

(972-2101)
(a) Histidine (b) Proline
(c) Tyrosine (d) Tryptophan

5. pH 11 (972-2101)
(a) arginine (b) aspartic acid
(c) glutamic acid (d) serine

6. --NH2-COOH pKa 10 2 pH
proton(962-2101)
(a) isomerization (b) neutralization
(c) zwitterions (d) stereoisomerization

7. (961-2101)
(A) L- form (B) L- form (C) D- form (D) D- form

8. 280 nm (952-2101)
(A) serine (B) tryptophan
(C) aspartic acid (D) methionine

9. (952-2101)
(A) gel filtration chromatography (B) isoelectric focusing (C) (C)
affinity chromatography (D) native gel electrophoresis

10. (951-2101)
(a) D form (b)
(c) (d) pH=7

11. trypsin(951-2101)
(a) phenylalanine (b) lysine
(c) methionine (d) aspartate
12. amino acidoptical isomer(942-5217)
(a) alanine (b) cysteine
(c) glutamic acid (d) glycine

13. (942-5217)
(a) tyrosine (b) aspartate
(c) tryptophan (d) histidine

14. histones DNA pI 10.8

(931-5217)
(A) ArgLys (B)AspGla
(C) ThrTyr (D) GlyPro

15. (pH) ? (901-015)

(a) Ala (b) Asn (c) Asp (d) Cys

16. side chainacidic group(912-5217)

(a) Arg (b) Asn (c) Asp (d) Lys

17. 280nm (92-5217)

(a) Tyrosine (b) Proline (c) Phenylalanine (d) Tryptophan

18. 280nm (91-3101)

(a) Ala (b) Cys (c) Met (d) Trp

19. (922-2101)
(a) GluVal (b) LysArg (c) LeuIle (d) GluAsp

20. pH7.0 peptideAla-Gly-Glu-Pro net charge(921-2101)

A 2 B1 C0 D1

21. ? (931-2101)
(a) (histidine) (b) (lysine) (c) (alanine) (d) (glutamate)

22. (932-2101)
A+H3N-CHCH3-COOH (b) H2N-CHCH3-COOH
C+H3N-CHCH3-COO- (d) H2N-CHCH3-COO-

23. Carbonic acid plasma pKa 6.1 plasma pH 7.1 HCO3-/H2CO3

(932-2101)
A100 : 1 (b) 1 : 100 (c) 1 : 10 (d) 10 : 1

24. pH 7.0 pentapeptide Ala-Asp-Leu-Glu-Lys (net charge) (941-2101)

A -1 (B) 0 (C) -2 (D) 1

25. SDS (92-5217)

(a)
(b) SDS
(c)
(d) SDS

26. ARVYIMPFNCBr
Dipeptide(922-2101)
(a) PF (b) AR (c) IM (d) VY
27. (912-5217)
A cyanogen bromide B6N HCl Cninhydrin DSanger reagent

28. N (921-2101)
ADansyl chloride B6N HCl CNinhydrin (?)DTrypsin

29. Edman reaction (922-2101)

A C B C D
phenylisothiocyanate

Protein structure and function

30. -helix(961-2101)
(A) proline (B) methionine
(C) tryptophan (D) histidine

31. collagen(952-2101)
(A) proline lysine modification
(B) Vitamin C
(C) glycinealanineproline
(D) hydroxylation

32. (951-2101)
(a) Disulfide bond
(b)
(c)
(d) helix

33. collagen(951-2101)
(a) collagen helix chainright-handed

(b) turnamino acid residues

(c) Glu-X-Y
(d) 4-hydroxyproline

34. -helix (931-5217)

(A) R group helix (B) helix turn 3.6A
(C) 3.6 helix turn (D)-helix hydrophobic interaction

35. (931-5217)
(A) electron microscopy (B) molecular model building (C) Ramachandran plot (D) X-ray diffraction

36. (91-3101)
ACyanogen bromide BSDSsodium dodecyl sulfate
Cprotease 37 D 110

37. Influenza virus hemagglutinin 60 helixhelix

(921-2101)
A4.5 nm B9.0 nm C18.0 nm D27.0 nm

38. Ramachandran Plots peptide backbone -60-50 (902-015)

A -turn B-helix C-sheet Drandom coil
39. Circular Dichroism (921-2101)
A B C D

40. helixhelix --------

RGPKIPSIATGMVGALLLLVVALGIGLFMRRRH-------- (921-2101)
ARGPKIPSIATGMVGALLL
BVALGIGLFMRRRH
CRGPKIPSIATGMVGALLLLVVALGIGLFMRRRH
DMVGALLLLVVALGIGLFM

41. turn ()?(921-2101)

A turn 2 Bturn 3
Cturn 4 Dturn 5

42. (91-3101)
Acircular dichroism Bfluorescence spectroscopy C
mass spectrometry DInfra Red spectroscopy

43. Watson Crick DNA (921-5217)

(a) UV (b) NMR (c) X-ray diffraction (d) IR

44. alpha (941-2101)

Adipole-dipole interaction (b) Van der Waals force
Chydrogen bond (d) electrostatic force

45. motif(922-2101)
A leucine zipper Bhelix-loop-helix Czinc finger Dcopper finger

46. ? (931-2101)
(a) glucosyl transferase (b) lysyl hydroxylase (c) lysyl oxidase
(d) prolyl hydroxylase

47. (scurvy)? (931-2101)

(a) (b) (c)
(d)

48. prion(91-3101)
A DNA BRNA Cprotein Dlipid

49. (911-5217)
A B C D

50. (proteoglycan)(931-2101)
A (fibronectin)B (keratin sulfate) C (gelatin) D (collagen)

Heme protein function

51. O 2,3-bisphosphoglycerate (982-2101)
2
(a) ketogenesis (b) glycolysis (c) gluconeogenesis (d)
pentose phosphate pathway

52. Hemoglobin T R (981-2101)

(a) O2 (b)Fe3+ (c) subunit association (d)
subunit dissociation
53.
CO(962-2101)
(a) Ccytochrome c (b) hemoglobin
(c) myoglobin (d) albumin

54. hemoprotein(91-3101)
AMyoglobin BCytochrome C CCytochrome p450 DDNase I

55. 7. (932-2101)
A50 (b) 200 (c) 2000 (d) 25000

56. (922-2101)
Acatalase Bcytochrome C Ccytochrome oxidase Dhemoglobin

57. (hemoglobin) ? (901-015)

(a) (methemoglobin) (Fe2+)
(b)
(c) (O2)
(d) , (myoglobin) C (cytochrome C) (heme)

58. , (oxygen dissociation curve) ,

: (901-015)
(a) (b) (c) (d)

59. : (931-2101)
(a) (b) (c) (d)

60. , ? (1) ; (2)

, ; (3) ; (4)
100 mmHg , 75% 80% . (931-2101)
(a) 1,2,3 (b) 1,3,4 (c) 1,2,4 (d) 2,3,4

61. (912-5217)
A B C DpH

62. (92-5217)

ACO2Hgb-CO2HCO3 BHCO3 Hgb-CO2CO2

CHgb-CO2HCO3 CO2 DHgb-CO2CO2HCO3

63. oxygen-hemoglobin dissociation curve (92-5217)

A CO2

B C 23diphosphoglycerateDPG D OH

64. (oxygen-hemoglobin dissociation curve) ? (941-2101)

(a) (b) (c) 2,3-DPG
(d)

65. (941-2101)
A (carbamino compound)
B
C
D
 Enzyme
66. G(981-2101)
(a) K'eq 1 G'o 0 (b) K'eq 1 G'o 0 (c) K'eq 1 G'o 1 (d)
G'o

67. competitive inhibitor (981-2101)

(a) Vmax (b) Km (c) VmaxKm (d) Km

68. double-reciprocal plotcompetitive inhibitor

(972-2101)
(a) 1/V (b) 1/[S] (c) V max (d) KpK

69. Alcohol dehydrogenaseEC 1.1.1.1alcoholaldehyde (971-

2101)
(a) transferase (b) oxidoreductase
(c) hydrolase (d) ligase

70. (971-2101)
(a) apoenzyme (b) coenzyme
(c) holoenzyme (d) zymogen

71. (951-2101)
(a) Km (b) Km
(c) (d) 100

72. (951-2101)
(a) (equilibrium constant
(b) activation energy
(c) standard free energy change
(d) initial velocity

73. substrate(942-5217)
(a) maximum velocity (b) dissociation constant
(c) coefficient of variation (d) turnover number

74. Chymotrypsin peptide bond

nucleophilic(942-5217)
(a) histidine 57 (b) aspartate 102 (c) serine 195 (d) cysteine 201

75. (932-5217)
(A) protein kinasephosphorylation
(B) trypsin
(C) competitive inhibitor
(D) allosteric regulation

76. Scatchard (932-5217)

(A) (B) ligand
(C) (D)

77. (931-5217)
(A) G (B) G (C) Keq (D) activation energy
78. Kcat / Km 2.4108(mol / L)-1 S-1
perfect enzyme(931-5217)
(A) hexokinase (B) lactate dehydrogense
(C) chymotrypsin (D) triose phosphate isomerase

79. protein kinasephosphatase(931-5217)

(A) glycogen synthase (B) HMG CoA reductase (C) phosphorylase b kinase (D) chymotrypsin

80. Metalloenzyme(92-5217)
A catalase Bglutathione peroxidase Celastase Dcarboxypeptidase A

81. pyruvate acetaldehyde ? (931-2101)

(a) (lyase) (b) (ligase) (c) (hydrolase)
(d) (oxidoreductase)

82. Michaelis-Menten steady state

(922-2101)
Asubstrate Benzyme CES complex Dproduct

83. substrate vs velocity Michaelis-Menten Equation(902-

015)
A kcat
BMichaelis Km
Ckcat/Kmenzyme efficiency
9
DVmax/Et 10

84. Km mol/l kcat s-1

chymotrypsin1.510-20.14pepsin310-40.5ribonuclease7.9
10-37.9102carbonic anhydrase2.610-64105substrate
efficiency(911-5217)
A chymotrypsin Bpepsin Cribonuclease Dcarbonic anhydrase

85. (I, II, III) :

Km(mM) Kcat (s-1)
I. PAPAG 4.0 26
II. PAPAA 1.5 37
III. PAPAF 0.64 18
0.5 mM ? (932-2101)
A I (b) II (c) III (d)

86. 2 specific activity 1 2

(921-2101)
AVmax1Vmax2 BKm1Km2
CVmax1/Km1Vmax2/Km2 DVmax1/Km1Vmax2/Km2

87. post-translation modificationreversible

(921-2101)
AADP-ribosylation Bglycosylation Cmyristoylation Dphosphorylation

88. (lactate dehydrogenase; LDH) , M H , LDH

? (901-015)
(a) 2 (b) 3 (c) 4 (d) 5

89. chymotrypsinogenchymotrypsin(962-2101)
(a) protein kinasephosphorylation.
(b) cAMP .
(c) ..
(d) proteolysis.

90. chymotrypsinogen chymotrypsin(912-5217)

A protein kinase chymotrypsinogen
2+
B Ca
C chymotrypsinogen chymotrypsin
Ddimertetramer

91. pepsin (922-2101)

E
F
G
H

92. (proteases) , ? (1) (chymotrypsinogen); (2)

(trypsinogen); (3) (trypsin); (4) (chymotrypsin). (931-2101)
(a) 1,4 (b) 2,3 (c) 3,4 (d) 1,2

93. A B C A B C
(91-3101)
A B C D

94. DFP (diisopropylfluorophosphate), ? (931-2101)

(a) Kinase (b) phosphatase (c) Cys protease (d) Ser protease

95. chymotrypsin irreversible inhibitor(922-2101)

Ap-nitrophenyl acetate Bdiisopropyl fluorophosphates
Ctosyl-L-lysine chloromethyl ketone DEDTA

96. (902-015)
Analoxone Bethanol Cmethadone Dlamotrigine

97. DiisopropylphosphofluoridateDIPF Chymotrypsin DIPF Chymotrypsin

(92-5217)
AAsp BHis CSer DVal

98. (pepsin) (941-2101)

A (HCl) (b) (trypsin) (c) (enteropeptidase)
D (amylase)

99. competitive inhibition(921-2101)

AKm Vmax BKm Vmax
CKm Vmax DKm Vmax

100. (uncompetitive inhibition) (941-2101)

AVmax Km (b) Vmax Km
CVmax Km (d) Vmax Km

101. Degradation(922-2101)
Amethylation Bglycosylation Cprenylation Dubiquitination
102. aspirin(911-5217)
A leukotriene Bprostaglandin Cacetylcholine D
epinephrine

103. Lovastatin HMG-CoA (941-2101)

Asuicide inhibitor (b) noncompetitive inhibitor
Cuncompetitive inhibitor (d) competitive inhibitor

104. prostaglandin H2 synthase (941-2101)

A (b) cyclooxygenase
C hydrophobic channel (d) aspirin

105. signal peptide(912-5217)

A N BC CN C D

106. alcohol dehydrogenase(912-5217)

A260nm B280nm C340nm D450nm

107. Lysozyme MN-acetylmuramateGN-acetylglucosamine(921-2101)

AMMMMMM BGMGMGM CMGMGMG DGGGGGG

108. (affinity) (941-2101)

Amyosin GDP actin
Bkinesin GTP microtubule
CG protein GDP effector
DG protein GDP G protein