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Questions and Answers
The net charge of the zwitterion form of Gly is .
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
The net charge of the zwitterion form of Gly is . A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
K
When a peptide bond is formed, an reacts with a carboxylate group.
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
When a peptide bond is formed, an reacts with a carboxylate group. A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
E
At a pH above its pK , the phenol group of tyrosine is
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
At a pH above its pK , the phenol group of tyrosine is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
C
In the tripeptide Lys─Pro─Ile, there are charged groups at pH 7.
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
In the tripeptide Lys─Pro─Ile, there are charged groups at pH 7. A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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At a pH below its pK , the -amino group of lysine is
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
At a pH below its pK , the -amino group of lysine is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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At a pH below its pK , the -carboxylate group of Asp is
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
At a pH below its pK , the -carboxylate group of Asp is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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In the peptide Trp─Ser─Val, valine is at the
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
In the peptide Trp─Ser─Val, valine is at the
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
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In the tripeptide Trp─Val─Phe, the N-terminal residue is
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
In the tripeptide Trp─Val─Phe, the N-terminal residue is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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In the tripeptide Lys─Pro─Ile, the C-terminal residue is
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
In the tripeptide Lys─Pro─Ile, the C-terminal residue is A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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Biological systems usually produce a single enantiomer, whereas chemical synthesis produces a
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
Biological systems usually produce a single enantiomer, whereas chemical synthesis produces a A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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GABA is a neurotransmitter derived from
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
GABA is a neurotransmitter derived from A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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Glutathione is a tripeptide containing a central. residue.
A) glutamate
B) uncharged
C) deprotonated
D) three
E) amino group
F) two
G) C-terminus
H) lysine
I) racemic mixture
J) cysteine
K) zero
L) protonated
M) isoleucine
N) tryptophan
O ) phenylalanine
P) N-terminus
Glutathione is a tripeptide containing a central. residue. A) glutamate B) uncharged C) deprotonated D) three E) amino group F) two G) C-terminus H) lysine I) racemic mixture J) cysteine K) zero L) protonated M) isoleucine N) tryptophan O ) phenylalanine P) N-terminus
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In the early 1930’s William Rose fed laboratory rats a mixture of all 19 amino acids known to be present in proteins. He observed that his rats lost weight. This observation led to the discovery of _ as the 20th amino acid found in proteins.
In the early 1930’s William Rose fed laboratory rats a mixture of all 19 amino acids known to be present in proteins. He observed that his rats lost weight. This observation led to the discovery of _ as the 20th amino acid found in proteins.
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What percentage of the 20 amino acids is considered to be nutritionally essential to lab animals?
What percentage of the 20 amino acids is considered to be nutritionally essential to lab animals?
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About half of the 20 amino acids are called essential because
About half of the 20 amino acids are called essential because
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Which amino acid does not have a primary -amino group?
Which amino acid does not have a primary -amino group?
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Which of the following statements is true?
Which of the following statements is true?
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Which of the following amino acids is the least abundant in proteins?
Which of the following amino acids is the least abundant in proteins?
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Zwitterions are
Zwitterions are
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The formation of a dipeptide from two amino acids involves
The formation of a dipeptide from two amino acids involves
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Which of the following amino acids has a charged polar side chain at pH 7.0?
Which of the following amino acids has a charged polar side chain at pH 7.0?
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Which of the following tripeptides carries a net positive charge at pH 7.0?
Which of the following tripeptides carries a net positive charge at pH 7.0?
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Which of the following amino acids has a sulfur atom in its side chain?
Which of the following amino acids has a sulfur atom in its side chain?
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Which of the following amino acids does not have an ionizable side chain
Which of the following amino acids does not have an ionizable side chain
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Which of the following amino acids has an uncharged polar side chain at pH 7.0?
Which of the following amino acids has an uncharged polar side chain at pH 7.0?
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The ionization of amino acids depends on the pH and the pK s of the ionizable groups.
The pK and pK for the amino acid shown above are 2.1 and 8.8, respectively. At what pH
is the amino acid ionized predominantly as shown?
The ionization of amino acids depends on the pH and the pK s of the ionizable groups. The pK and pK for the amino acid shown above are 2.1 and 8.8, respectively. At what pH is the amino acid ionized predominantly as shown?
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The pK1 , pK 2, and pKr for the amino acid arginine are 1.8, 9.0, and 12.5, respectively.
At pH 7.0 arginine would be charged predominantly as follows:
The pK1 , pK 2, and pKr for the amino acid arginine are 1.8, 9.0, and 12.5, respectively.
At pH 7.0 arginine would be charged predominantly as follows:
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The pK1 , pK 2, and pKr for the amino acid aspartic acid are 2.0, 9.9, and 3.9, respectively.
At pH 7.0, aspartic acid would be charged predominantly as follows:
The pK1 , pK 2, and pKr for the amino acid aspartic acid are 2.0, 9.9, and 3.9, respectively.
At pH 7.0, aspartic acid would be charged predominantly as follows:
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The pK 1, pK2 , and pK rfor the amino acid glutamate are 2.1, 9.5, and 4.1, respectively.
At pH 11.0, glutamate would be charged predominantly as follows:
The pK 1, pK2 , and pK rfor the amino acid glutamate are 2.1, 9.5, and 4.1, respectively.
At pH 11.0, glutamate would be charged predominantly as follows:
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While proteins are usually composed of linear chains of amino acids, branched chains of amino acids and internally cross-linked chains can be found in certain proteins. Polypeptide chains are most commonly linked to each other through
While proteins are usually composed of linear chains of amino acids, branched chains of amino acids and internally cross-linked chains can be found in certain proteins. Polypeptide chains are most commonly linked to each other through
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The disulfide bond between two cysteine molecules
The disulfide bond between two cysteine molecules
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The tripeptide glycylarginylglutamate contains four ionizable groups with pK s of 2.1,
a
4.1 9.8, and 12.5. Calculate the pI for this molecule.
The tripeptide glycylarginylglutamate contains four ionizable groups with pK s of 2.1, a 4.1 9.8, and 12.5. Calculate the pI for this molecule.
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The tripeptide alanyllysylaspartate contains four ionizable groups with pK s of 2.0, 3.9,
a
9.9, and 10.5. Calculate the pI for this molecule.
The tripeptide alanyllysylaspartate contains four ionizable groups with pK s of 2.0, 3.9, a 9.9, and 10.5. Calculate the pI for this molecule.
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The isoelectronic point of an amino acid is the point where
The isoelectronic point of an amino acid is the point where
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The side-chains of amino acids have
The side-chains of amino acids have
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The peptide AYDG has an N-terminal residue.
The peptide AYDG has an N-terminal residue.
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Which of the following tripeptides would be expected to be the most hydrophobic?
Which of the following tripeptides would be expected to be the most hydrophobic?
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What is the three-letter abbreviation for the peptide valylarginylisoleucine?
What is the three-letter abbreviation for the peptide valylarginylisoleucine?
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Ribosomes use L amino acids to synthesize proteins. These amino acids are called “L” because
Ribosomes use L amino acids to synthesize proteins. These amino acids are called “L” because
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Ribosomes use L amino acids to synthesize proteins. These amino acids are called “L” because
Ribosomes use L amino acids to synthesize proteins. These amino acids are called “L” because
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Which of the amino acids represented below has two chiral centers?
Which of the amino acids represented below has two chiral centers?
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All the standard amino acids except are optically active.
All the standard amino acids except are optically active.
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The character of most standard amino acids causes solutions of amino acids to rotate the plane of polarized light.
The character of most standard amino acids causes solutions of amino acids to rotate the plane of polarized light.
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All amino acids derived from proteins have the same stereochemical conformation as.
All amino acids derived from proteins have the same stereochemical conformation as.
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Typically, modified amino acids, those with side chain modifications that are present in proteins
Typically, modified amino acids, those with side chain modifications that are present in proteins
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An amide bond between a side-chain carboxylate and an -amino group is also called a(n)
An amide bond between a side-chain carboxylate and an -amino group is also called a(n)
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