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Kailash Institute of Chemical Sciences 30/03/15

SHEET : 1 (AMINO ACIDS)


1. Which amino acid is least likely to be found in a natural protein?

2. Which amino acid is unlikely to be found in a natural protein?

3. Which of these amino acids has the R configuration at the stereogenic center but, nonetheless, is an
L amino acid?

4. Which of these amino acids cannot be described as an L amino acid?

5. Which of these amino acids is a D amino acid?

6. Which of these amino acids is an R amino acid?

7. Which of the following amino acids is theoretically capable of existing in diastereomeric forms?

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Kailash Institute of Chemical Sciences 30/03/15

8. Which amino acid is achiral?

9. Disulfide bonds in proteins:


A) result from an oxidation of thiols. B) help to maintain the shape of proteins.
C) can be broken by reduction. D) can link two cysteine amino acid residues.
E) All of the above
10. Which amino acid would have its isoelectric point near pH 10?

11. Which amino acid would have its isoelectric point near pH 3?

12. Which amino acid would have its isoelectric point near pH 10?

13. Which amino acid would have its isoelectric point near pH 10?
Glycine Tryptophan Serine Proline Lysine
14. Which amino acid would not have its isoelectric point in the pH range 5-7?
A) Leucine B) Threonine C) Methionine D) Arginine
E) Cysteine

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Kailash Institute of Chemical Sciences 30/03/15

15. Which amino acid would not have its isoelectric point in the pH range 5-7?
A) Glycine B) Proline C) Cysteine D) Glutamine
E) All of these amino acids have isoelectric point in the pH range 5-7
16. What might be concluded upon determining that an unknown amino acid has its isoelectric point
near pH 10?
A. It must have a hydrophobic side chain B. It must have a hydrophilic side chain
C. Its side chain must contain more basic groups then acidic functions
D. Its side chain must contain an acidic group
17. What might be concluded upon determining that an unknown amino acid has its isoelectric point
near pH 3?
A. It must have a hydrophobic side chain B. It must have a hydrophilic side chain
C. Its side chain must contain a basic group D. Its side chain must contain more acidic groups
then basic groups
18. The pH at which the concentration of the dipolar ion (zwitterion) form of an amino acid is at a
maximum and the cationic and anionic forms are at equal concentrations is termed the
A. end point. B. equivalence point. C. neutral point. D. isoelectric point.
E. dipolar point.
19. What is the pI of the following amino acid?

20. What is the pI of the following amino acid?

21. What is the pI of the following amino acid?

22. . What is the pI of the following amino acid?

23. What would be the predominant form of lysine in water at pH 14?

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Kailash Institute of Chemical Sciences 30/03/15

24. The predominant form of aspartic acid in water at pH 1 would be:

25. For the accompanying fully-protonated amino acid, what is the arrangement of pKa
values in order of increasing magnitude?
CO2H
HO2C
III
I NH3
II
26. Which of these amino acids contains a hydrophobic side chain?
A) Lysine B) Serine C) Methionine D) Arginine E) Cysteine
27. Which of these natural amino acids contains an amide function?
A) Asparagine B) Proline C) Arginine D) Histidine
28. Which of these natural amino acids contains a heterocyclic ring?
A) Asparagine B) Proline C) Arginine D) Histidine E) B and D
29. Which of these natural amino acids contains an amide function?
A) Asparagine B) Methionine C) Cysteine D) Glutamine
E) Two of these
30. Which of these natural amino acids contains two carboxylic acid groups?
A) Cystine B) Cysteine C) Glutamic acid D) A and B
E) A and C
31. Which of these natural amino acids contains a phenolic group?
A) Phenylalanine B) Tyrosine C) Tryptophan D) 4-Hydroxyproline
E) Serine
32. Which of these natural amino acids contains a pyrrolidine ring?
A) Phenylalanine B) Tyrosine C) Tryptophan D) 4-Hydroxyproline
33. Which of these natural amino acids contains an indole ring?
Phenylalanine Tyrosine Tryptophan 4-Hydroxyproline Asparigine
34. Which of these natural amino acids contains an imidazole ring?
A) Histidine B) Lysine C) Tryptophan D) 4-Hydroxyproline
35. Which of these natural amino acids contains an –OH group?

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Kailash Institute of Chemical Sciences 30/03/15

A) Serine B) Threonine C) Tyrosine D) Two of these E) All


36. Which of these natural amino acids, when present in a polypeptide, is likely to exhibit significant
hydrogen bonding through its side chain?
Serine Threonine Tyrosine Two of these All of these
37. Which of these natural amino acids, when present in a polypeptide, is not likely to exhibit
significant hydrogen bonding through its side chain?
Leucine Threonine Tyrosine Serine
All of these are likely to exhibit significant hydrogen bonding through the side chain
38. Which of these amino acids is formed from a precursor amino acid only after the latter has been
incorporated into a polypeptide chain?
A) Serine B) Arginine C) Isoleucine D) Tryptophan
E) Hydroxyproline
39. Which of these amino acids is described as an “essential” amino acid?
A) Methionine B) Phenylalanine C) Isoleucine D) Tryptophan
E) All of these are “essential” amino acids
40. Pipecolic acid logically would be substituted for which natural amino acid in the synthesis of
peptide analogs?

NH Pipecolic acid

CO2H

Histidine Proline Tryptophan Phenylalanine Tyrosine


41. Logically, the following “unnatural” amino acid would be substituted for which natural amino
acid in the synthesis of peptide analogs?
HO CO2H
NH2

Tyrosine Proline Tryptophan Phenylalanine Histidine


42. Logically, the following “unnatural” amino acid would be substituted for which natural amino
acid in the synthesis of peptide analogs?
CO2H
NH2
HS

A) Methionine B) Cysteine C) Cystine D) Tyrosine


E) It could be substituted for all of these amino acids
43. Logically, the following “unnatural” amino acid would be substituted for which natural amino
acid in the synthesis of peptide analogs?

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Kailash Institute of Chemical Sciences 30/03/15

HO2C CO2H
NH2

Aspartic acid Glutamine Lysine Asparagine Glutamic acid


44. Which is an isolable intermediate in the Strecker synthesis of an amino acid?

45. Which of the following would provide a synthesis of alanine?


A) CH2=CHCH2OH, HBr, CrO3/H2SO4/H2O; then xs NH3
B) Potassium phthalimide, ClCH2CO2C2H5; then KOH/H2O; then HCl
C) Potassium phthalimide, C6H5CH2Br; then KOH/H2O; then CO2,H3O+
D) CH3CH2COOH, (C6H5)3CNa; then NH3
E) Answers A) and B)
46. Which of the following would provide a synthesis of valine?
A) (CH3)2C=CHCH2OH, HBr/peroxides; CrO3/H2SO4/H2O; then xs NH3
B) Potassium phthalimide, (CH3)2CHCHClCO2C2H5; then KOH/H2O; then HCl
C) Potassium phthalimide, (CH3)2CHCH2Br; then KOH/H2O; then CO2,H3O+
D) CH3CH2COOH, (C6H5)3CNa; then NH3
E) Answers A) and B)
47. Which of the following would provide a synthesis of leucine?
A) (CH3)2C=CHCH2OH, HBr/peroxides, CrO3/H2SO4/H2O; then excess NH3
B) Potassium phthalimide, BrCH(CO2C2H5)2; (CH3)2CHCHClCO2C2H5; then KOH/H2O;
then HCl (85%), heat
C) Potassium phthalimide, BrCH(CO2C2H5)2; (CH3)2CHCH2Br; then KOH/H2O; then HCl
(85%), heat
D) (CH3)2CHCOOH, PCl5; then NH3
E) Answers A) and C)
48. Which of the following would provide a synthesis of phenylalanine?
A) Phenylacetaldehyde, NH3, HCN; H3O+, heat
B) Potassium phthalimide, BrCH(CO2C2H5)2; C6H5CH2Br; then KOH/H2O; then HCl (85%), heat
C) Potassium phthalimide, (C6H5)CH2CH2Br; then KOH/H2O; then HCl (85%), heat
D) C6H5CH2COOH, SOCl2; then NH3
E) Answers A) and B)

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Kailash Institute of Chemical Sciences 30/03/15

49. What product(s) would you expect from the following reaction?
H2O
Tyrosine + Br2 (excess) ?

50. Why is this sequence, CH2=CHCH2OH + HBr, then CrO3/H2SO4/H2O, finally xs NH3, not a
good method for the preparation of L-alanine?
A) NH3 is not sufficiently nucleophilic to perform the final step.
B) HBr does not add to substituted alkenes.
C) 1° alcohols are not oxidized by CrO3 in acidic solution.
D) Initial HBr addition produces a racemic intermediate which leads to racemic product.
E) Steric hindrance precludes nucleophilic substitution at a 2° carbon atom.
51. Which one of these amino acids does not give the usual purple color with ninhydrin?
Histidine Proline Tryptophan Leucine Aspartic acid
52. The purple color of the anion formed in the ninhydrin test for α-amino acids is due to:
A) the attraction of the anion to a metal in a pi-complex.
B) intermolecular hydrogen bonding. C) molecular vibrations.
D) the highly conjugated nature of the anion. E) the color of the ninhydrin.
53. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the
pentapeptide gives: Val•Asp, Glu•His, Phe•Val, and Asp•Glu. What is the amino acid sequence of
the pentapeptide?
A. Phe•Val•Asp•Glu•His B. His•Glu•Asp•Val•Phe
C. Asp•Glu•His•Phe•Val D. Phe•Val•Glu•His•Asp E. Glu•His•Phe•Val•Asp
54. A heptapeptide Ala2, Glu, Phe, Pro, Tyr, Val gives labeled alanine when heated with DNFB
followed by hydrolysis. On partial hydrolysis the unlabeled heptapeptide gives the following:
Ala•Glu, Pro•Tyr, Ala•Val, Tyr•Ala, Val•Phe•Pro.
What is the amino acid sequence of the heptapeptide?
A. Ala•Phe•Pro•Tyr•Ala•Glu•Val B. Ala•Val•Phe•Pro•Tyr•Ala•Glu
C. Ala•Val•Phe•Pro•Tyr•Glu•Ala D. Ala•Val•Phe•Tyr•Pro•Ala•Glu
E. Val•Ala•Phe•Tyr•Pro•Ala•Glu
55. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene (and base) and then
subjected to acidic hydrolysis, which amino acid will bear the dinitrophenyl group?

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Kailash Institute of Chemical Sciences 30/03/15

When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene (and base) and then
subjected to acidic hydrolysis, which amino acid will bear the dinitrophenyl group?
Leu•Val•Gly•Phe•Ile
A) Leucine B)Valine C)Glycine D)Phenylalanine E)Isoleucine
56. The Edman degradation uses this reagent to identify the N-terminal amino acid of a peptide or
protein.
C6H5NHNH2 C6H5NH2 C6H5N=C=S C6H5N=C=O
Aminopeptidase
57. The primary structure of a protein refers to its:
A) sequence of amino acid residues. B) disulfide bonds. C) helical structure.
D) hydrogen bonding. E) All of these
58. How many different tripeptides can exist, each containing one residue of glycine, one of L-
threonine, and one of L-arginine?
A. 2 B. 3 C. 6 D. 8 E. 9
59. Which amino acid of a polypeptide would become labeled when the polypeptide is treated with
2,4-dinitrofluorobenzene in base, even though the amino acid is not a terminal amino acid?
A. Lysine B. Glycine C. Alanine D. Phenylalanine E. Leucine
60. Which of these is used to convert a protein into smaller, more manageable fragments for
subsequent structural studies?
A) Insulin B) Aminopeptidase C) Carboxypeptidase D Trypsin which is produced in the
pancreas as the inactive proenzyme trypsinogen. E) 2,4-Dinitrofluorobenzene
61. This reagent is used to "protect" the amino group of an amino acid which is to be joined to a
second amino acid by a peptide bond.
CH3 O O CH3
H3C CH3
O O
H3C O O O CH3

A. Cl B. C6H5 Cl C. (Boc2O)

O O O

D. C6H5 O C6H5 E. O Cl

62. Why is dicyclohexylcarbodiimide (DCC) used in peptide synthesis?


A) DCC "protects" the amino group of the intended N-terminal amino acid.
B) DCC activates the carboxyl group of one amino acid so that this amino acid reacts more
readily with a second amino acid.
C) DCC cleaves the blocking groups from the final peptide.
D) DCC is the resin used in the automated synthesis of peptides.
E) DCC removes the peptide from the resin at the conclusion of the synthesis.

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Kailash Institute of Chemical Sciences 30/03/15

63. What product would be obtained upon treating alanine with the following reagent ?
O
O Cl

64. The secondary structure of proteins is derived from:


A) peptide linkages. B) disulfide linkages. C) hydrogen bond formation.
D) hydrophobic interactions. E) acid-base interactions.
65. Which attractive force is responsible for maintaining the tertiary structure of a protein?
A) Disulfide linkages B) Hydrogen bonds C) van der Waals forces
D) Hydrophobic interactions E) All of these
66. The occurrence of this amino acid in a polypeptide chain disrupts an α-helix:
A) Proline B) Alanine C) Methionine D) Histidine E) Tyrosine
67. A "conjugated protein" is one which:
A) possesses catalytic properties. B) is a digestive enzyme.
C) exists largely as an α-helix. D) contains unsaturated amino acids.
E) contains a nonprotein group as part of the molecule.
68. What is the configuration on all steric centers in these aminoacids
COOH COOH
H2N H H2N H
H3C H H OH
CH2CH3 CH3

69. . Draw the structures of the predominant forms of the amino acids in the mixture at given pH:
A) glycine (pI = 6.0) and Lysine (pI = 9.7) at pH = 7.
B) phenylalanine (pI = 5.5) leucine (pI = 6) at pH = 6.
Predict the direction of migration (toward anode or cathode) of these amino acids during
electrophoresis at given Ph
70. Predict the direction of migration (toward anode or cathode) of alanine during electrophoresis at
pH = 5.
71. Draw structures to represent what happens when valine is dissolved in a strongly acidic solution
(pH=0).
72. Draw the structures of the following amino acids as they would appear in solution of pH = 3.
A) lysine, B) glutamic acid, C) alanine, D) glycine.

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Kailash Institute of Chemical Sciences 30/03/15

73. Draw the structures of the following amino acids as they would appear in solution of pH = 10.
A) lysine, B) glutamic acid, C) alanine, D) glycine.
74. Show the structure of the amino acids corresponding to these three-letter codes:
A) Trp B) Ile C) Cys D) His
75. 84. The amino acid threonine, (2S, 3R)-2-amino-3-hydroxybutanoic acid, has two chiral
centers. Draw a Fisher projection of threonine.
76. Draw the scheme of the reaction of GlyCys with H2O2
77. Draw the structures of the predominant forms of glycine at pH = 2.0, 6.0, and 10. Indicate the
direction of migration (toward anode or cathode) for each structure.
78. Draw the structure of L-phenylalanine and L-valine in Fischer projection.
79. For the following statements, please answer either true or false:
A) Proteins are high molecular weight natural polymers made up largely by combination of various α-
amino acids. true/false
B) Amino acids may be classified according to properties as: neutral, basic and acidic. true/false
C) Amino acids may be grouped under a nutritive classification into two categories: essential and
nonessential. true/false
D) Amino acids have an isoelectric point. true/false
E) Proteins, when hydrolyzed, yield amino acids and polypeptides. true/false
F) Proteins are easily precipitated, or coagulated, by heat, by acids, and by certain heavy metals.
true/false
80. Amino acids can be prepared from aldehydes by treatment with ammonia and HCN followed by
hydrolysis. This method is known as the-----
81. Beginning with a three-carbon alcohol, outline all necessary steps in the preparation of D,L-
alanine.
82. Complete the following equations:
H3 C COOH
A) + NaNO2 + HCl
NH 2

O
B) Ph + H 2NCH2 COOH
Cl

H3 C COOH
C) + NaOH
NH 2

H3 C COOH
D) + CH3OH + HCl
NH 2

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Kailash Institute of Chemical Sciences 30/03/15

83. What are the name and the structure of the products A and B?
CH3
O 1. Br2, P NH3, (excess)
H3C A B
OH 2. H2O

4-methylpentanoic acid

84. Show how a Strecker synthesis might be used to prepare phenylalanine starting from
phenylacetldehyde
85. Complete the reaction presented below

H3N
SH ICH2-COOH

COO-

86. What is the final product formed when potassium phthalimide is subjected to the following
reaction sequence? Give structural details of all significant intermediates, including stereochemistry,
as applicable.

O i. BrCH(CO2H5)2
ii. NaOEt, C6H5CH2Br
N K ?
iii. NaOH
O iv. HCl, heat
87. Give the structure of the aldehyde which, upon treatment with HCN and ammonia, followed by
heating with aqueous acid, would afford racemic tryptophan. What is this strategy for the synthesis of
α -amino acids called?
88. What is the final product formed via the following reaction sequence? Give structural details of
all significant intermediates.
CO2Et i. CH2=CHCN, NaOEt, EtOH
HN ?
CO2Et ii. conc HCl, reflux
O

89. A reagent that reacts with most amino acids to give an intense purple color is called _____.
90. Show the structures of the products obtained on reaction of valine with ninhydrin
91. The most widely used method for identifying the N-terminal amino acid in a peptide chain is
called the - - - - -
92. C-terminal amino acids can be identified through the use of
93. Draw the structure of the following tripeptide (starting with the N-terminal residue and ending
with the C-terminal residue), showing stereochemical details: Gly-Phe-Met
94. Draw the structure of the following tripeptide (starting with the N-terminal residue and ending
with the C-terminal residue), showing stereochemical details: Ala-Ser-Leu

95. Suggest a reasonable strategy for the synthesis of the dipeptide Leu-Phe, using established
protocol for peptide synthesis

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