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Deck 26: Biomolecules: Amino Acids,peptides,and Proteins
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Question
Question
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an amino acid in its zwitterionic form.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an amino acid in its zwitterionic form.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
Question
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a carboxyl-protected amino acid.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a carboxyl-protected amino acid.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
Question
Question
Question
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an octapeptide with a C-terminal valine.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an octapeptide with a C-terminal valine.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
Question
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a polypeptide which gives four fragments on treatment with chymotrypsin.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a polypeptide which gives four fragments on treatment with chymotrypsin.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
Question
Question
Question
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ the product of an Edman degradation.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ the product of an Edman degradation.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
Question
Question
Question
Question
Question
Question
Question
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a peptide coupling reagent.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a peptide coupling reagent.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
Question
Question
Question
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ small organic molecules which act as coenzymes.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ small organic molecules which act as coenzymes.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
Question
Consider the following titration curve for an amino acid. 
What is the pI of this amino acid?
A)A
B)B
C)D
D)F
What is the pI of this amino acid?A)A
B)B
C)D
D)F
Question
Question
Draw and name the structure of the tripeptide formed from the following amino acids.Use B as the N-terminal acid and A as the C-terminal end.Atoms other than carbon and hydrogen are labeled. 
A B C
A B C Question
What alkyl halide should be used to prepare the following amino acid by the amidomalonate method? Atoms other than carbon and hydrogen are labeled. 
Question
Question
Consider the following image. 
Which level of protein structure is shown here?
A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Which level of protein structure is shown here?A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Question
The following amino acid: (Atoms other than carbon and hydrogen are labeled. ) 
A)has two chirality centers.
B)is classified as secondary α-amino acid.
C)is characterized by three pKas
D)would have a net +1 charge as shown.
A)has two chirality centers.
B)is classified as secondary α-amino acid.
C)is characterized by three pKas
D)would have a net +1 charge as shown.
Question
Consider the following image. 
Which level of protein structure is shown in the box?
A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Which level of protein structure is shown in the box?A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Question
Question
Question
Question
Consider the following titration curve for an amino acid. 
At which of the following "pH" values would the amino acid have a net charge of zero?
A)A
B)B
C)D
D)F
At which of the following "pH" values would the amino acid have a net charge of zero?A)A
B)B
C)D
D)F
Question
Show how you could prepare the following amino acid starting with the appropriate carboxylic acid.Atoms other than carbon and hydrogen are labeled. 
Question
Classify the following amino acid.Atoms other than carbon and hydrogen are labeled. 
A)acidic
B)basic
C)neutral
A)acidic
B)basic
C)neutral
Question
Consider the following image. 
Which level of protein structure is shown here?
A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Which level of protein structure is shown here?A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Question
Question
Consider the following titration curve for an amino acid. 
At which of the following "pH" values would the amino acid be fully deprotonated?
A)A
B)B
C)D
D)F
At which of the following "pH" values would the amino acid be fully deprotonated?A)A
B)B
C)D
D)F
Question
Question
Which of the following is a correct representation of the amino acid below? Atoms other than carbon and hydrogen are labeled. 
A)Isoleucine
B)ILe
C)I
D)None of these present this amino acid.
E)All of these represent this amino acid.
A)Isoleucine
B)ILe
C)I
D)None of these present this amino acid.
E)All of these represent this amino acid.
Question
On the titration curve for an amino acid.In terms of the letters on the graph,label the isoelectric point,the pKa of the amino group and the pKa of the carboxyl group. 
Question
The enzyme that would catalyze the following reaction 
would belong in which classification?
A)kinase
B)oxidase
C)protease
D)transaminase
would belong in which classification?A)kinase
B)oxidase
C)protease
D)transaminase
Question
Consider the image below. 
What type of interaction is indicated by the arrow?
A)Salt bridges
B)Disulfide bonds
C)Hydrogen bonds
D)Dispersion forces
What type of interaction is indicated by the arrow?A)Salt bridges
B)Disulfide bonds
C)Hydrogen bonds
D)Dispersion forces
Question
Question
Question
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Deck 26: Biomolecules: Amino Acids,peptides,and Proteins
1
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Show how leucine might be synthesized using the Knowles enantioselective synthesis.
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Show how leucine might be synthesized using the Knowles enantioselective synthesis.
2
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an amino acid in its zwitterionic form.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an amino acid in its zwitterionic form.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
3
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a carboxyl-protected amino acid.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a carboxyl-protected amino acid.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
4
Exhibit 26-4
Refer to the data below to answer the following question(s):
Porcine dynorphin is a neuropeptide having 17 amino acid residues.Its structure is shown below.
Tyr−Gly−Gly−Phe−Leu−Arg−Arg−Ile−Arg−Pro−Lys−Leu−Lys−Trp−Asp−Asn−Gln
Refer to Exhibit 26-4.Leu5-enkephalin is a pentapeptide contained as the N-terminal sequence of dynorphin.Write the structure of Leu5-enkephalin using both the three letter and one letter abbreviations for the amino acids.
Refer to the data below to answer the following question(s):
Porcine dynorphin is a neuropeptide having 17 amino acid residues.Its structure is shown below.
Tyr−Gly−Gly−Phe−Leu−Arg−Arg−Ile−Arg−Pro−Lys−Leu−Lys−Trp−Asp−Asn−Gln
Refer to Exhibit 26-4.Leu5-enkephalin is a pentapeptide contained as the N-terminal sequence of dynorphin.Write the structure of Leu5-enkephalin using both the three letter and one letter abbreviations for the amino acids.
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5
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw the structure of the predominant form of leucine at pH = 1.50.
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw the structure of the predominant form of leucine at pH = 1.50.
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6
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an octapeptide with a C-terminal valine.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ an octapeptide with a C-terminal valine.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
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7
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a polypeptide which gives four fragments on treatment with chymotrypsin.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a polypeptide which gives four fragments on treatment with chymotrypsin.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
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8
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw the structure of the predominant form of leucine at pH = 10.00.
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw the structure of the predominant form of leucine at pH = 10.00.
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9
The most acidic amino acid is ____.
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10
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ the product of an Edman degradation.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ the product of an Edman degradation.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
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11
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.How many possible stereoisomers of leucine are there?
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.How many possible stereoisomers of leucine are there?
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12
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Leucine is described as an essential amino acid.What does this mean?
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Leucine is described as an essential amino acid.What does this mean?
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13
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw the condensed structure for leucine,and label all chirality centers with an asterisk.
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw the condensed structure for leucine,and label all chirality centers with an asterisk.
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14
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw a Fischer projection of L-leucine and label the chirality center(s) as R or S.
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Draw a Fischer projection of L-leucine and label the chirality center(s) as R or S.
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15
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Show the alkyl halide you would use to prepare leucine by the amidomalonate method.
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.Show the alkyl halide you would use to prepare leucine by the amidomalonate method.
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16
Exhibit 26-1
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.What is the pI of leucine?
Refer to the data below to answer the following question(s):
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid.It has pKa1 = 2.36 and pKa2 = 9.60.
Refer to Exhibit 26-1.What is the pI of leucine?
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17
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a peptide coupling reagent.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ a peptide coupling reagent.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
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18
The most basic amino acid is _____.
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19
Define isoelectric point.
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20
Exhibit 26-2
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ small organic molecules which act as coenzymes.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
MATCH a structure from the list below to each of the following terms.Place the letter of the structure in the blank to the left of the term which it describes.
_____ small organic molecules which act as coenzymes.
A)
B)
C)
Val−Phe−Leu−Met−Tyr−Pro−Gly−Trp−Cys−Glu
D)
E)
F) Asp−Tyr−Ile−His−Pro−Phe−Arg−Val
G)
apoenzyme
H)
I)
J)
K)
L) Val−Lys−Phe−Gly−Arg−Met−Arg−Phe
M) vitamins
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21
Consider the following titration curve for an amino acid. What is the pI of this amino acid?
A)A
B)B
C)D
D)F
What is the pI of this amino acid?A)A
B)B
C)D
D)F
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22
Exhibit 26-4
Refer to the data below to answer the following question(s):
Porcine dynorphin is a neuropeptide having 17 amino acid residues.Its structure is shown below.
Tyr−Gly−Gly−Phe−Leu−Arg−Arg−Ile−Arg−Pro−Lys−Leu−Lys−Trp−Asp−Asn−Gln
Refer to Exhibit 26-4.What fragments would result if dynorphin were cleaved by trypsin?
Refer to the data below to answer the following question(s):
Porcine dynorphin is a neuropeptide having 17 amino acid residues.Its structure is shown below.
Tyr−Gly−Gly−Phe−Leu−Arg−Arg−Ile−Arg−Pro−Lys−Leu−Lys−Trp−Asp−Asn−Gln
Refer to Exhibit 26-4.What fragments would result if dynorphin were cleaved by trypsin?
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23
Draw and name the structure of the tripeptide formed from the following amino acids.Use B as the N-terminal acid and A as the C-terminal end.Atoms other than carbon and hydrogen are labeled. A B C
A B C Unlock Deck
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24
What alkyl halide should be used to prepare the following amino acid by the amidomalonate method? Atoms other than carbon and hydrogen are labeled.
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25
Exhibit 26-5
Refer to the data below to answer the following question(s):
The octapeptide saralasin is a specific antagonist of angiotensin II.A derivative of saralasin is used therapeutically as an antihypertensive.Amino acid analysis of saralasin show the presence of the following amino acids:
Ala,Arg,His,Pro,Sar,Tyr,Val,Val
Refer to Exhibit 26-5.Sar is the abbreviation for sarcosine,N-methyl aminoethanoic acid.Draw the structure of sarcosine.
Refer to the data below to answer the following question(s):
The octapeptide saralasin is a specific antagonist of angiotensin II.A derivative of saralasin is used therapeutically as an antihypertensive.Amino acid analysis of saralasin show the presence of the following amino acids:
Ala,Arg,His,Pro,Sar,Tyr,Val,Val
Refer to Exhibit 26-5.Sar is the abbreviation for sarcosine,N-methyl aminoethanoic acid.Draw the structure of sarcosine.
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26
Consider the following image. Which level of protein structure is shown here?
A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Which level of protein structure is shown here?A)Primary
B)Secondary
C)Tertiary
D)Quaternary
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27
The following amino acid: (Atoms other than carbon and hydrogen are labeled. )
A)has two chirality centers.
B)is classified as secondary α-amino acid.
C)is characterized by three pKas
D)would have a net +1 charge as shown.
A)has two chirality centers.
B)is classified as secondary α-amino acid.
C)is characterized by three pKas
D)would have a net +1 charge as shown.
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28
Consider the following image. Which level of protein structure is shown in the box?
A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Which level of protein structure is shown in the box?A)Primary
B)Secondary
C)Tertiary
D)Quaternary
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29
Show the steps involved in a synthesis of the peptide "F-G-I" using the Merrifield procedure.
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30
Exhibit 26-4
Refer to the data below to answer the following question(s):
Porcine dynorphin is a neuropeptide having 17 amino acid residues.Its structure is shown below.
Tyr−Gly−Gly−Phe−Leu−Arg−Arg−Ile−Arg−Pro−Lys−Leu−Lys−Trp−Asp−Asn−Gln
Refer to Exhibit 26-4.What fragments would result if dynorphin were cleaved by chymotropsin?
Refer to the data below to answer the following question(s):
Porcine dynorphin is a neuropeptide having 17 amino acid residues.Its structure is shown below.
Tyr−Gly−Gly−Phe−Leu−Arg−Arg−Ile−Arg−Pro−Lys−Leu−Lys−Trp−Asp−Asn−Gln
Refer to Exhibit 26-4.What fragments would result if dynorphin were cleaved by chymotropsin?
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31
How many different peptides could be produced using one each of the following amino acids? Ala,Gly,His,Cys
A)6
B)16
C)24
D)64
A)6
B)16
C)24
D)64
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32
Consider the following titration curve for an amino acid. At which of the following "pH" values would the amino acid have a net charge of zero?
A)A
B)B
C)D
D)F
At which of the following "pH" values would the amino acid have a net charge of zero?A)A
B)B
C)D
D)F
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33
Show how you could prepare the following amino acid starting with the appropriate carboxylic acid.Atoms other than carbon and hydrogen are labeled.
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34
Classify the following amino acid.Atoms other than carbon and hydrogen are labeled.
A)acidic
B)basic
C)neutral
A)acidic
B)basic
C)neutral
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35
Consider the following image. Which level of protein structure is shown here?
A)Primary
B)Secondary
C)Tertiary
D)Quaternary
Which level of protein structure is shown here?A)Primary
B)Secondary
C)Tertiary
D)Quaternary
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36
Consider the following data for a hypothetical basic amino acid. pKa
3)15
8)22
10)93
What is the pI of this substance?
A)5.68
B)7.04
C)8.22
D)9.58
3)15
8)22
10)93
What is the pI of this substance?
A)5.68
B)7.04
C)8.22
D)9.58
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37
Consider the following titration curve for an amino acid. At which of the following "pH" values would the amino acid be fully deprotonated?
A)A
B)B
C)D
D)F
At which of the following "pH" values would the amino acid be fully deprotonated?A)A
B)B
C)D
D)F
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38
Exhibit 26-5
Refer to the data below to answer the following question(s):
The octapeptide saralasin is a specific antagonist of angiotensin II.A derivative of saralasin is used therapeutically as an antihypertensive.Amino acid analysis of saralasin show the presence of the following amino acids:
Ala,Arg,His,Pro,Sar,Tyr,Val,Val
Refer to Exhibit 26-5.N-Terminal analysis by the Edman method shows saralasin contains sarcosine at the N-terminus.Partial hydrolysis of saralasin with dilute hydrochloric acid yields the following fragments:
Tyr−Val−His
Sar−Arg−Val
His−Pro−Ala
Val−Tyr−Val
Arg−Val−Tyr
What is the structure of saralasin?
Refer to the data below to answer the following question(s):
The octapeptide saralasin is a specific antagonist of angiotensin II.A derivative of saralasin is used therapeutically as an antihypertensive.Amino acid analysis of saralasin show the presence of the following amino acids:
Ala,Arg,His,Pro,Sar,Tyr,Val,Val
Refer to Exhibit 26-5.N-Terminal analysis by the Edman method shows saralasin contains sarcosine at the N-terminus.Partial hydrolysis of saralasin with dilute hydrochloric acid yields the following fragments:
Tyr−Val−His
Sar−Arg−Val
His−Pro−Ala
Val−Tyr−Val
Arg−Val−Tyr
What is the structure of saralasin?
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39
Which of the following is a correct representation of the amino acid below? Atoms other than carbon and hydrogen are labeled.
A)Isoleucine
B)ILe
C)I
D)None of these present this amino acid.
E)All of these represent this amino acid.
A)Isoleucine
B)ILe
C)I
D)None of these present this amino acid.
E)All of these represent this amino acid.
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40
On the titration curve for an amino acid.In terms of the letters on the graph,label the isoelectric point,the pKa of the amino group and the pKa of the carboxyl group.
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41
The enzyme that would catalyze the following reaction would belong in which classification?
A)kinase
B)oxidase
C)protease
D)transaminase
would belong in which classification?A)kinase
B)oxidase
C)protease
D)transaminase
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42
Consider the image below. What type of interaction is indicated by the arrow?
A)Salt bridges
B)Disulfide bonds
C)Hydrogen bonds
D)Dispersion forces
What type of interaction is indicated by the arrow?A)Salt bridges
B)Disulfide bonds
C)Hydrogen bonds
D)Dispersion forces
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43
The coenzymes NAD+ and FAD are involved in:
A)acyl transfer.
B)methyl transfer.
C)decarboxylation.
D)oxidation/reduction.
A)acyl transfer.
B)methyl transfer.
C)decarboxylation.
D)oxidation/reduction.
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44
Which of the following contributes most substantially to rate acceleration produced by an enzyme?
A)Ability to bind the substrate
B)Ability to bind the transition state
C)Ability to bind the product
D)All of the above contribute equally.
A)Ability to bind the substrate
B)Ability to bind the transition state
C)Ability to bind the product
D)All of the above contribute equally.
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45
Which level of protein structure is disrupted upon mild heating or alteration in pH?
A)Primary
B)Secondary
C)Tertiary
A)Primary
B)Secondary
C)Tertiary
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