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2. Amino acids
Page: 72 Difficulty: 2 Ans: B
Of the 20 standard amino acids, only ___________ is not optically active. The reason is that its side
chain ___________.
A)
B)
C)
D)
E)
3. Amino acids
Page: 72 Difficulty: 1 Ans: C
Two amino acids of the standard 20 contain sulfur atoms. They are:
A)
B)
C)
D)
E)
4. Amino acids
Page: 75 Difficulty: 1 Ans: A
All of the amino acids that are found in proteins, except for proline, contain a(n):
A)
B)
C)
D)
E)
amino group.
carbonyl group.
carboxyl group.
ester group.
thiol group.
5. Amino acids
22
Pages: 7576
Difficulty: 3 Ans: C
Which of the following statements about aromatic amino acids is correct?
A)
B)
C)
D)
8. Amino acids
Pages: 7879
Difficulty: 1 Ans: A
Amino acids are ampholytes because they can function as either a(n):
A)
B)
C)
D)
E)
acid or a base.
neutral molecule or an ion.
polar or a nonpolar molecule.
standard or a nonstandard monomer in proteins.
transparent or a light-absorbing compound.
9. Amino acids
23
Pages: 7980
Difficulty: 2 Ans: D
Titration of valine by a strong base, for example NaOH, reveals two pKs. The titration reaction
occurring at pK2 (pK2 = 9.62) is:
A)
B)
C)
D)
E)
COOH + OH
COOH + NH2
COO + NH2+
NH3+ + OH
NH2 + OH
COO + H2O.
COO + NH2+.
COOH + NH2.
NH2 + H2O.
NH + H2O.
NH2CH2COOH.
NH2CH2COO .
NH2CH3+COO .
NH3+CH2COOH.
NH3+CH2COO .
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1
1
2
cleavage
condensation
group transfer
isomerization
oxidation reduction
a disulfide bridge.
five peptide bonds.
four peptide bonds.
no free carboxyl group.
two free amino groups.
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Larger proteins have a more uniform distribution of amino acids than smaller proteins.
Proteins contain at least one each of the 20 different standard amino acids.
Proteins with different functions usually differ significantly in their amino acid composition.
Proteins with the same molecular weight have the same amino acid composition.
The average molecular weight of an amino acid in a protein increases with the size of the protein.
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carbohydrates.
flavin nucleotides.
lipids.
metals .
phosphates.
cytochrome c
immunoglobulin G
ribonuclease A
RNA polymerase
serum albumin
Mr = 13,000
Mr = 145,000
Mr = 13,700
Mr = 450,000
Mr = 68,500
contains a denaturing detergent that can distribute uniform negative charges over the proteins surface.
exhibits a stable pH gradient when ampholytes become distributed in an electric field.
is washed with an antibody specific to the protein of interest.
neutralizes all ionic groups on a protein by titrating them with strong bases.
relates the unknown protein to a series of protein markers with known molecular weights, Mr.
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Primary structure
Secondary structure
Tertiary structure
Quaternary structure
None of the above
Primary structure
Secondary structure
Tertiary structure
Quaternary structure
None of the above
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GlyPheLysLysGlyLeuMetPheHis.
HisLeuGlyLysLysPhePheGlyMet.
HisLeuPheGlyLysLysPheMetGly.
HisPheLeuGlyLysLysPheMetGly.
MetLeuPheLysPheGlyGlyLysHis.
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30
Difficulty: 2
A
B
C
D
E
__________________________________________________________________
Tyr-Lys-Met Gly-Pro-Arg
Asp-Trp-Tyr
Asp-His-Glu
Leu-Val-Phe
Which one of the above tripeptides:
____(a) is most negatively charged at pH 7?
____(b) will yield DNP-tyrosine when reacted with l-fluoro-2,4-dinitrobenzene and
hydrolyzed in acid?
____(c) contains the largest number of nonpolar R groups?
____(d) contains sulfur?
____(e) will have the greatest light absorbance at 280 nm?
Ans: (a) D; (b) A; (c) E; (d) A; (e) C
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pH = pKa + log
[conjugate base]
[acid]
pKa pH = log
[acid]
[conjugate base]
[acid]
[conjugate base]
[acid]
[conjugate base]
4 = [acid]/[conjugate base], or
4[conjugate base] = [acid]
Therefore, at pH 5.4, 4/5 (80%) of the histidine will be in the protonated form.
51. Amino acids
Page: 80 Difficulty: 2
The amino acid histidine has three ionizable groups, with pKa values of 1.8, 6.0, and 9.2. (a) Which
pKa corresponds to the histidine side chain? (b) In a solution at pH 5.4, what percentage of the
histidine side chains will carry a positive charge?
Ans: (a) 6.0; (b) 80%. (See the previous problem for expanded solution to this problem.)
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34
35
protein A
7.4
82,000
yes
protein B
3.8
21,500
yes
protein C
7.9
23,000
no
protein X
7.8
22,000
yes
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37
___ hydrolysis of peptide bonds on the carboxyl side of Lys and Arg
___ cleavage of peptide bonds on the carboxyl side of Met
___ breakage of disulfide (SS) bonds
___ determination of the amino acid sequence of a peptide
___ determining the amino-terminal amino acid in a polypeptide
Ans: g; a; d and e; b; c
70. The covalent structure of proteins
Pages: 94-97
Difficulty: 2
A biochemist wishes to determine the sequence of a protein that contains 123 amino acid residues.
After breaking all of the disulfide bonds, the protein is treated with cyanogen bromide (CNBr), and it
is determined that that this treatment breaks up the protein into seven conveniently sized peptides,
which are separated from each other. It is your turn to take over. Outline the steps you would take to
determine, unambiguously, the sequence of amino acid residues in the original protein.
Ans: (1) Use Edman degradation to determine the sequence of each peptide. (2) Create a second set
of peptides by treatment of the protein with a specific protease (e.g., trypsin), and determine the
sequence of each of these. (3) Place the peptides in order by their overlaps. (4) Finally, by a similar
analysis of the original protein without first breaking disulfide bonds, determine the number and
location of SS bridges.
71. The covalent structure of proteins
Pages: 94-97
Difficulty: 3
You are trying to determine the sequence of a protein that you know is pure. Give the most likely
explanation for each of the following experimental observations. You may use a simple diagram for
your answer.
(a) The Sanger reagent (FDNB, fluorodinitrobenzene) identifies Ala and Leu as aminoterminal residues, in roughly equal amounts.
(b) Your protein has an apparent Mr of 80,000, as determined by SDS-polyacrylamide gel
electrophoresis. After treatment of the protein with performic acid, the same technique
reveals two proteins of Mr 35,000 and 45,000.
(c) Size-exclusion chromatography (gel filtration) experiments indicate the native protein has
an apparent Mr of 160,000.
Ans: (a) The protein has some multiple of two subunits, with Ala and Leu as the amino-terminal
residues. (b) The protein has two subunits (Mr 35,000 and 45,000), joined by one or more disulfide
bonds. (c) The native protein (Mr 160,000) has two Mr 35,000 subunits and two Mr 40,000 subunits.
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