Organic Chemistry, 8e (Wade)

Chapter 24 Amino Acids, Peptides, and Proteins

1) Peptide bonds are:
A) ester linkages.
B) imido linkages.
C) ether linkages.
D) amide linkages.
E) disulfide linkages.
Answer: D
Diff: 1
Section: 24.1
2) Which of the standard amino acids is achiral?
A) lysine
B) proline
C) valine
D) alanine
E) glycine
Answer: E
Diff: 1
Section: 24.2
3) How many standard amino acids are there?
A) 4
B) 12
C) 20
D) 30
E) 64
Answer: C
Diff: 1
Section: 24.2
4) Which of the following amino acids has its -carbon as part of a 5-membered ring?
A) proline
B) tryptophan
C) histidine
D) tyrosine
E) phenylalanine
Answer: A
Diff: 1
Section: 24.2

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5) Which of the following amino acids has a nonpolar side chain?

A) serine
B) aspartic acid
C) asparagine
D) threonine
E) leucine
Answer: E
Diff: 1
Section: 24.2
6) Which amino acid has a phenol in its side chain?
A) tyrosine
B) tryptophan
C) isoleucine
D) asparagine
E) histidine
Answer: A
Diff: 1
Section: 24.2
7) Which amino acid has an amide group in its side chain?
A) tyrosine
B) tryptophan
C) isoleucine
D) asparagine
E) histidine
Answer: D
Diff: 1
Section: 24.2
8) Which amino acid has an imidazole ring in its side chain?
A) tyrosine
B) tryptophan
C) isoleucine
D) asparagine
E) histidine
Answer: E
Diff: 1
Section: 24.2

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9) Which amino acid has an indole ring in its side chain?

A) tyrosine
B) tryptophan
C) isoleucine
D) asparagine
E) histidine
Answer: B
Diff: 1
Section: 24.2
10) Which of the following amino acids does not contain an aromatic R-group?
A) tyrosine
B) phenylalanine
C) tryptophan
D) histidine
E) none of the above
Answer: E
Diff: 1
Section: 24.2
11) Proteins which provide all the essential amino acids in about the right proportions are called:
A) globular proteins.
B) enzymes.
C) complete proteins.
D) glycoproteins.
E) nucleoproteins.
Answer: C
Diff: 1
Section: 24.2
12) Which of the following terms best describes the side chain of valine?
A) acidic
B) basic
C) charged, polar
D) uncharged, polar
E) nonpolar
Answer: E
Diff: 2
Section: 24.2

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13) Nearly all naturally occurring amino acids:

A) are racemic mixtures.
B) are achiral.
C) have the (R) configuration at the -carbon.
D) have the (S) configuration at the -carbon.
E) have basic side chains.
Answer: D
Diff: 2
Section: 24.2
14) Which of the following amino acids has a side chain which contains a nonbasic nitrogen?
A) proline
B) glutamine
C) histidine
D) tyrosine
E) lysine
Answer: B
Diff: 2
Section: 24.2
15) Which of the following amino acids does not have an aromatic substructure within its side chain?
A) tryptophan
B) tyrosine
C) phenylalanine
D) histidine
E) proline
Answer: E
Diff: 2
Section: 24.2
16) What is the one letter symbol of the amino acid below?

A) G
B) Q
C) W
D) R
E) M
Answer: B
Diff: 2
Section: 24.2
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17) What is the one letter symbol of the amino acid below?

A) G
B) Q
C) W
D) T
E) F
Answer: C
Diff: 2
Section: 24.2
18) Provide the Fischer projection of L-aspartic acid.
Answer:

Diff: 2
Section: 24.2
19) Provide the single letter code for the following peptide
Arg-Phe-Tyr-Cys-Asp-Trp-Gln-Ala-Glu-Glu-His-Lys
Answer: RFYCDWQAEEHK
Diff: 2
Section: 24.2
20) If the side chain of asparagine is hydrolyzed, what amino acid is formed?
Answer: aspartic acid
Diff: 2
Section: 24.2
21) Most naturally occurring amino acids are L-amino acids. Does this mean they are levorotatory?
Explain.
Answer: No, this does not mean they are levorotatory. The "L" designation arises because the amino
group is on the left in the Fischer projection and thus correlates to L-glyceraldehyde. The direction of
optical rotation must be determined experimentally.
Diff: 2
Section: 24.2
22) Which of the following amino acids are classified as essential amino acids?
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(More than one answer is possible.)

A) isoleucine
B) proline
C) tryptophan
D) histidine
Answer: A, C, D
Diff: 2
Section: 24.2
23) Amino acids have:
A) high melting points and low solubility in water.
B) large dipole moments and are more acidic than most carboxylic acids.
C) high melting points and large dipole moments.
D) low solubility in water and small dipole moments.
E) small dipole moments and are hydrophobic.
Answer: C
Diff: 1
Section: 24.3
24) Which of the following reagents can be used to convert disulfide bridges into cysteic acid residues?
A) HCO3H
B) Zn, HCl
C) PhNCS
D) PhCH2OCOCl
E) CH3I
Answer: A
Diff: 2
Section: 24.3
25) Addition of alanine to distilled water will produce:
A) a slightly basic solution.
B) denaturation.
C) a neutral solution.
D) a slightly acidic solution.
E) hydrolysis.
Answer: D
Diff: 2
Section: 24.3

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26) Which amino acid's side chain is positively charged at biological pH?
A) arginine
B) tyrosine
C) aspartic acid
D) serine
E) glutamine
Answer: A
Diff: 2
Section: 24.3
27) Which amino acid's side chain is negatively charged at biological pH?
A) arginine
B) tyrosine
C) aspartic acid
D) serine
E) glutamine
Answer: C
Diff: 2
Section: 24.3
28) Draw the form of L-lysine which is present at biological pH.
Answer:

Diff: 2
Section: 24.3
29) Draw structures for the forms of glycine present in basic, neutral, and acidic solutions.
Answer:
Diff: 2
Section: 24.3
30) Provide the structure of L-arginine at pH 2.0.
Answer:

Diff: 2
Section: 24.3

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31) Provide the structure of L-valine at pH 12.0.

Answer:

Diff: 2
Section: 24.3
32) Provide the structure of L-aspartic acid at pH 12.0.
Answer:

Diff: 2
Section: 24.3
33) Provide the structure of the predominant form of alanine present in an aqueous solution at a pH of
2.0.
Answer:

Diff: 2
Section: 24.3

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34) Provide the structure of the predominant form of lysine present in an aqueous solution at biological
pH.
Answer:

Diff: 2
Section: 24.3
35) Provide the structure of the predominant form of glutamine present in an aqueous solution at a pH of
12.0.
Answer:

Diff: 2
Section: 24.3
36) Draw the Fischer projection of L-valine at a pH of 12.
Answer:

Diff: 2
Section: 24.3
37) Draw the Fischer projection of L-valine at a pH of 2.
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Answer:

Diff: 2
Section: 24.3
38) Draw the Fischer projection of L-glutamic acid at a pH of 12.
Answer:

Diff: 2
Section: 24.3
39) Draw the Fischer projection of L-glutamic acid at a pH of 2.
Answer:

Diff: 2
Section: 24.3
40) Draw the form of L-tryptophan which is present at biological pH.
Answer:

Diff: 2
Section: 24.3

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41) What is the net charge of arginine in a solution of pH 10.0?

Answer: -1
Diff: 2
Section: 24.3
42) Provide the structure of the predominant form of L-valine present in an aqueous solution at
biological pH.
Answer:

Diff: 2
Section: 24.3
43) Provide the structure of the predominant form of L-phenylalanine present in an aqueous solution at
biological pH.
Answer:

Diff: 2
Section: 24.3
44) Provide the structure of the predominant form of L-methionine present in an aqueous solution at
biological pH.
Answer:

Diff: 2
Section: 24.3
45) Provide the structure of the predominant form of L-leucine present in an aqueous solution at pH 2.
Answer:

Diff: 2
Section: 24.3

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46) Given the following pKa values, what is the major ionization state of histidine at pH 11?
(-COOH = 2.0, -NH3+ = 9.0 and R-group imine = 6.5)
A)

B)

C)

D)

E)

Answer: E
Diff: 3
Section: 24.3
47) Provide the structure of the predominant form of L-alanine present in an aqueous solution at pH 2.
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Answer:

Diff: 2
Section: 24.3
48) A solution of glycine has a pH equal to the pKa1 of glycine. What forms of glycine are present and
in what ratio?
Answer:

cationic,

zwitterionic

Diff: 3
Section: 24.3
49) The isoelectric point is important in:
A) the enzymatic resolution of amino acids.
B) electrophoresis.
C) determination of the C-terminal amino acid.
D) determination of the N-terminal amino acid.
E) the ninhydrin test.
Answer: B
Diff: 1
Section: 24.4
50) Which of the following amino acids has its isoelectric point at the highest pH?
A) glycine
B) aspartic acid
C) valine
D) arginine
E) methionine
Answer: D
Diff: 2
Section: 24.4
51) Which of the following amino acids has its isoelectric point at the lowest pH?
A) arginine
B) aspartic acid
C) valine
D) glycine
E) methionine
Answer: B
Diff: 2
Section: 24.4

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52) Which of the following amino acids has an isoelectric pH of 3.2?

A) glycine
B) asparagine
C) lysine
D) glutamic acid
E) methionine
Answer: D
Diff: 2
Section: 24.4
53) In an electrophoresis carried out at pH 9.0, does phenylalanine migrate toward the cathode, migrate
toward the anode, or not migrate at all? Explain briefly.
Answer: At pH 9.0 phenylalanine has a net charge of -1. This anionic species thus migrates toward the
positively charged anode.
Diff: 2
Section: 24.4
54) Describe how electrophoresis works.
Answer: A sample of an amino acid mixture is placed in the center of an acrylamide gel. Two electrodes
are placed in contact with the edges of the gel and a high electrical potential is applied across the
electrodes. Based on their charge, species then migrate through the gel toward the appropriate electrode
and are thereby separated.
Diff: 2
Section: 24.4
55) What is the isoelectric point of lysine within in +/- 1 pH unit?
A) 3
B) 6
C) 9
D) 12
Answer: C
Diff: 2
Section: 24.4
56) Which of the following amino acids has its isoelectric point at the highest pH?
A) glycine
B) aspartic acid
C) valine
D) lysine
E) methionine
Answer: D
Diff: 2
Section: 24.4

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57) Which of the following amino acids has its isoelectric point at the lowest pH?
A) arginine
B) glutamic acid
C) valine
D) glycine
E) methionine
Answer: B
Diff: 2
Section: 24.4
58) Provide a reasonable synthesis of racemic alanine from ethanol.
Answer:
1. PCC
2. NH3, HCN
3. H3O+
Diff: 1
Section: 24.5
59) Provide a synthesis of racemic valine from 3-methylbutanoic acid.
Answer:
1. Br2, PBr3
2. H2O
3. excess NH3
4. H3O+
Diff: 2
Section: 24.5
60) Provide a reasonable synthesis of PhCH2CH(NH3+)CO2H from BrCH(CO2CH2CH3)2.
Answer:
1. potassium phthalimide
2. NaOCH2CH3
3. PhCH2Br
4. H3O+,
Diff: 2
Section: 24.5
61) How can an -ketoacid be converted to an -aminoacid?
Answer: Treat with excess NH3 to generate the imine, then reduce this intermediate with H2, Pd.
Diff: 2
Section: 24.5

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62) Provide the necessary reagents to convert propionic acid to alanine.

Answer:

Diff: 2
Section: 24.5
63) Show how 3-methylthiopropanal may be converted to methionine.

Answer:

Diff: 2
Section: 24.5
64) In biosynthesis, which amino acid serves as the source of the amino group for other amino acids?
A) D-phenylalanine
B) L-phenylalanine
C) racemic phenylalanine
D) L-glutamic acid
E) D-glutamic acid
Answer: D
Diff: 3
Section: 24.5

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65) What is the name of the amino acid produced when propanoic acid is subjected to the following
sequence of reagents: 1. PBr3, Br2; 2. H2O; 3. NH3, ?
A) alanine
B) aspartic acid
C) glutamic acid
D) valine
E) asparagine
Answer: A
Diff: 3
Section: 24.5
66) What is the major end product of the following reaction series?

A) Ala
B) Gly
C) Leu
D) Ile
E) Val
Answer: E
Diff: 3
Section: 24.5
67) Show the step-wise synthesis of glutamic acid starting with -ketoglutarate and ammonia.
Answer:

Diff: 3
Section: 24.5
68) Provide a synthesis of isoleucine from N-phthalimidomalonic ester.
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Answer:
1. NaOCH2CH3
2. CH3CHBrCH2CH3
3. H3O+,
Diff: 3
Section: 24.5
69) Provide a detailed, stepwise mechanism for the Strecker synthesis of racemic alanine from
acetaldehyde.
Answer:

Diff: 3
Section: 24.5
70) Suggest a method for resolving a racemic acid.
Answer: Make diastereomeric salts by reaction with an optically pure acid or base. Separate
diastereomers via selective crystallization.
or
Acylate the amino acids and then treat with hog kidney acylase. This enzyme will selectively hydrolyze
the acyl group in the L-amino acid derivative.
Diff: 2
Section: 24.6
71) Which of the following will result in removal of a benzyl ester protecting group?
A) acid hydrolysis only
B) decarbonylation only
C) catalytic hydrogenation only
D) both acid hydrolysis and decarbonylation
E) both catalytic hydrogenation and acid hydrolysis
Answer: E
Diff: 2
Section: 24.7

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72) Which of the following reagents are commonly used to acylate the amino group of an amino acid?
A) both acetic anhydride and benzyl chloroformate
B) both benzyl chloroformate and -bromoacetic acid
C) both -bromoacetic acid and tosyl chloride
D) both tosyl chloride and acetic anhydride
E) both benzyl chloroformate and tosyl chloride
Answer: A
Diff: 2
Section: 24.7
73) Provide the major organic product in the reaction of L-methionine with benzyl chloroformate.
Answer:

Diff: 2
Section: 24.7
74) Provide the structure of the major organic product which results when L-phenylalanine is treated
with a large excess of PhCH2OH and gaseous HCl.
Answer:

Diff: 2
Section: 24.7
75) Which of the following indicators is commonly used to visualize bands of amino acids?
A) ninhydrin
B) bromocresol green
C) potassium permanganate
D) vanillin dip
Answer: A
Diff: 2
Section: 24.7
76) A polypeptide was treated with a certain enzyme to yield the following amino acid sequences. What
enzyme was used to induce the observed fragmentations?
Val-Pro-Phe

Leu-Ser-Lys-Glu-Trp

Arg-Ile-Ser-Ser-Leu-Tyr

Answer: Chymotrypsin
Diff: 2
Section: 24.7
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77) Amides are:

A) the most reactive acid derivative.
B) the most acidic acid derivative.
C) the most stable acid derivative.
D) the least stable acid derivative.
E) both A and D
Answer: C
Diff: 1
Section: 24.8
78) Disulfide linkages can form between:
A) two cysteine residues.
B) two methionine residues.
C) a cysteine residue and a methionine residue.
D) two threonine residues.
E) a methionine residue and a threonine residue.
Answer: A
Diff: 1
Section: 24.8
79) The nonprotein part of a conjugated protein is called a ________ group.
Answer: prosthetic
Diff: 1
Section: 24.8
80) Draw the dipeptide Val-Tyr.
Answer:

Diff: 2
Section: 24.8
81) Draw the structure of the tetrapeptide Ser-Leu-Phe-Pro.
Answer:

Diff: 2
Section: 24.8

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82) Provide a structure of the dipeptide Ala-Ser at biological pH.

Answer:

Diff: 2
Section: 24.8
83) Provide a structure of the dipeptide Ile-Gln at biological pH.
Answer:

Diff: 2
Section: 24.8
84) Draw the structure of Lys-Phe-Leu at biological pH.
Answer:

Diff: 2
Section: 24.8

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85) Draw the structure of Val-Ala-Ser at biological pH.

Answer:

Diff: 2
Section: 24.8
86) Provide the structure of Thr-Gln-Met.
Answer:

Diff: 2
Section: 24.8
87) Provide a structure of the dipeptide Ser-Gly-Asp at biological pH.
Answer:

Diff: 2
Section: 24.8
88) Provide a structure of the dipeptide Val-Lys-Glu at biological pH.
Answer:

Diff: 2
Section: 24.8

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89) Provide a structure of the dipeptide Gly-Asp-Leu at biological pH.

Answer:

Diff: 2
Section: 24.8
90) Which of the following amino acids has its isoelectric point at the highest pH?
A) glutamic acid
B) lysine
C) serine
D) histisdine
E) cysteine
Answer: B
Diff: 2
Section: 24.8
91) When a disulfide linkage is formed, the compound containing this new linkage has been ________.
A) oxidized
B) reduced
C) electrolyzed
D) hydrolyzed
E) dehydrated
Answer: A
Diff: 2
Section: 24.8
92) The term ________ is sometimes used to describe peptides which contain four to ten amino acid
residues.
Answer: oligopeptide
Diff: 2
Section: 24.8
93) Which of the following compounds would reduce a disulfide linkage in a peptide?
A) urea
B) concentrated NaOH
C) dithiothreitol
D) dilute HCl
E) bromine
Answer: C
Diff: 1
Section: 24.9

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94) An amino acid analyzer can be used to determine:

A) the sequence of amino acids in a peptide.
B) the identity of the amino acids present in a peptide.
C) the relative amounts of the amino acids present in a peptide.
D) both A and C
E) both B and C
Answer: E
Diff: 2
Section: 24.9
95) The reagent used in the determination of the N-terminal amino acid residue of a peptide is:
A) carboxypeptidase.
B) phenyl isothiocyanate.
C) dicyclohexylcarbodiimide.
D) ethyl chloroformate.
E) peroxyformic acid.
Answer: B
Diff: 2
Section: 24.9
96) What compound is also known as Sanger reagent, and how is it used in peptide structure
determination?
Answer: 2,4-dinitrofluorobenzene; used in determining the N-terminal residue
Diff: 2
Section: 24.9
97) Show where trypsin would cleave the peptide shown below.

Answer:

Diff: 2
Section: 24.9
98) Show where chymotrypsin would cleave the peptide shown below.

Answer:

Diff: 2
Section: 24.9

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99) Show the mechanism for the hydrolysis of the following dipeptide?

Answer:

Diff: 2
Section: 24.9
100) Before Edman degradation, Fredrick Sanger developed the first method to analyze the N-terminal
amino acid of a protein using 2,4-dinitrofluorobenzene in the following reaction. Propose a mechanism
for this reaction.

Answer: Classic Nucleophilic Aromatic Substitution reaction.

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Diff: 2
Section: 24.9
101) How is the enzyme chymotrypsin used in peptide structure determination?
Answer: Chymotrypsin cleaves the peptide chain at the carboxyl groups of phenylalanine, tyrosine, and
tryptophan. Each of these shortened chains is then sequenced and the original peptide is sequenced by
determining fragment overlap.
Diff: 2
Section: 24.9
102) Treatment of a peptide which contains disulfide linkages with peroxyformic acid yields a peptide
which contains what new amino acid residue?
A) cystine
B) cysteic acid
C) 4-hydroxyproline
D) -alanine
E) methioic acid
Answer: B
Diff: 3
Section: 24.9
103) What peptide remains after two sequential Edman degradations of the pentapeptide
A) Pro-Gly-Phe
B) Ser-Pro-Gly
C) Gly-Phe-Arg
D) Pro-Gly
E) Phe-Arg
Answer: C
Diff: 3
Section: 24.9

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104) What is the practical limit on the use of carboxypeptidase in providing sequence information?
A) two residues on the C-terminal end
B) two residues on the N-terminal end
C) three residues on the N-terminal end
D) three residues on the C-terminal end
E) six residues on the N-terminal end
Answer: A
Diff: 3
Section: 24.9
105) Which of the following fragments would not result when the decapeptide Asn-Gly-Lys-Phe-ProArg-Gly-Leu-Lys-Ser is treated with trypsin?
A) Gly-Leu-Lys
B) Phe-Pro-Arg
C) Asn-Gly-Lys
D) Pro-Arg-Gly-Leu
Answer: D
Diff: 3
Section: 24.9
106) When the structure of a small dipeptide was examined using NMR, it was observed that the
carbonyl oxygen atoms in the backbone structure are nearly always trans with respect to the H atoms on
the amide nitrogens. Explain this observation and include diagrams.
Answer: Apparently the extra unshared electrons on the nitrogen atoms are shared with the carbonyl
carbon in a resonance hybrid structure. The resulting hybrid structure would have significant double
bond characteristic that would inhibit free rotation around the amide bond. The hindred rotation
apparently favors the trans configuration of the carbonyl oxygen and the amide hydrogen atoms.

Diff: 3
Section: 24.9

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107) Complete hydrolysis of a hexapeptide gives 2 Gly, Leu, Phe, Pro, and Tyr. Reaction of the peptide
with phenylisothiocyanate gave the phenylthiohydantoin of Pro. Partial hydrolysis of the peptide gave
the following fragments: Phe-Gly-Tyr, Gly-Phe-Gly, Pro-Leu-Gly, Leu-Gly-Phe. What is the structure of
the peptide?
Answer: Pro-Leu-Gly-Phe-Gly-Tyr
Diff: 3
Section: 24.9
108) Bradykinin is a nonapeptide released by globulins in the blood in response to a wasp sting.
Hydrolysis gives the following amino acids: 2 Arg, Gly, 2 Phe, 3 Pro, and Ser. Edman degradation gives
phenylthiohydantoin of Arg. Cleavage with carboxypeptidase gives Arg. Partial hydrolysis gives the
following di- and tripeptides: Phe-Ser, Pro-Gly-Phe, Pro-Pro, Ser-Pro-Phe, Phe-Arg, and Arg-Pro. What
is the amino acid sequence of bradykinin?
Answer: Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Diff: 3
Section: 24.9
109) Chymotrypsin is an enzyme which cleaves a peptide chain at the carboxyl groups of three aromatic
amino acid residues. Name these three.
Answer: phenylalanine, tyrosine, and tryptophan
Diff: 3
Section: 24.9
110) Which of the following reagents is used to protect the amino group of the N-terminal residue in
solution-phase peptide synthesis?
A) lithium diisopropyl amide
B) benzyl chloroformate
C) phenyl isothiocyanate
D) dicyclohexylcarbodiimide
E) trifluoroacetic acid
Answer: B
Diff: 2
Section: 24.10
111) Provide the structure of the major organic product which results when L-histidine is treated with
benzyl chloroformate.
Answer:

Diff: 2
Section: 24.10

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112) Provide a reasonable synthesis of Gly-Val from the individual amino acids.
Answer:
1. Glycine + benzyl chloroformate gives N-protected Z-Gly.
2. Z-Gly is activated with ethyl chloroformate.
3. Activated Z-Gly is treated with Val to form Z-Gly-Val.
4. Benzyloxycarbonyl protecting group is removed via catalytic hydrogenation to give Gly-Val.
Diff: 3
Section: 24.10
113) The solid-phase method of peptide synthesis was devised by:
A) Sanger
B) Merrifield
C) Edman
D) Strecker
E) Lister
Answer: B
Diff: 1
Section: 24.11
114) What peptide coupling reagent is most commonly used in solid phase peptide synthesis?
Answer: dicyclohexylcarbodiimide (DCC)
Diff: 2
Section: 24.11
115) Give a detailed, stepwise mechanism for the formation of the activated acyl derivative from the
reaction of an amino acid with N,N'-dicyclohexylcarbodiimide.
Answer:

Diff: 3
Section: 24.11

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116) A protein bonded to a sugar residue would be classified as a:

A) simple protein.
B) glycoprotein.
C) lipoprotein.
D) metalloprotein.
E) nucleoprotein.
Answer: B
Diff: 1
Section: 24.12
117) A protein bonded to a fat would be classified as a:
A) simple protein.
B) glycoprotein.
C) lipoprotein.
D) metalloprotein.
E) nucleoprotein.
Answer: C
Diff: 1
Section: 24.12
118) Which of the following is not an example of a protein?
A) hemoglobin
B) keratin
C) insulin
D) cholesterol
E) snake venom
Answer: D
Diff: 1
Section: 24.12
119) Which type of protein, globular or fibrous, tends to function primarily as structural parts of an
organism?
Answer: fibrous
Diff: 2
Section: 24.12

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120) Show how a monosaccharide such as glucose can attach to a protein structure through the
formation of an O-linked glycosidic bond with Ser. (Hint: This structure would be properly called an
acetal.)
Answer:

Diff: 3
Section: 24.12
121) The primary structure of a protein refers to:
A) the sequence of its amino acids.
B) the orientation of -helices.
C) the orientation of pleated sheets.
D) the orientation of peptide subunits within a complex protein.
E) the placement of the protein's active site.
Answer: A
Diff: 1
Section: 24.13
122) Which of the following arrangements is usually not found in the secondary structure of proteins?
A) -helix
B) double helix
C) random coil
D) pleated sheet
Answer: B
Diff: 1
Section: 24.13
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123) The H-bonds formed in the tertiary structure of proteins can be differentiated from those formed in
secondary structures. What is the major distinguishing factor?
A) The H-bonds in 3 structures are significantly stronger than those found in 2 structures.
B) The H-bonds in 3 structures are more random than those formed in 2 structures.
C) The H-bonds in 3 structures are formed by predictable interactions among the peptide backbone amine and -carboxylate groups.
D) The H-bonds in 3 structures are formed by interactions involving the side chain R-groups.
E) Both B and D are correct.
Answer: E
Diff: 2
Section: 24.13
124) What is the major force responsible for the formation of an -helix in protein secondary structure?
Answer: hydrogen bonding
Diff: 2
Section: 24.13
125) In a globular protein, would the side chain of aspartic acid most probably be oriented toward the
interior of the protein or outward toward the aqueous surroundings? Explain.
Answer: The aspartic acid side chain is negatively charged at biological pH. This negatively charged
group is highly hydrophilic and will most likely be oriented to the exterior so that interaction with water
is possible.
Diff: 2
Section: 24.13
126) What name is given to a protein infectious agent that is thought to promote misfolding and
polymerization of normal protein molecules and that is believed to cause Creutzfeldt-Jakob Disease?
Answer: prion protein
Diff: 1
Section: 24.14
127) ________ of a protein usually results in the precipitation of the protein and loss of its biological
activity.
Answer: Denaturation
Diff: 2
Section: 24.14

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