Rutgers Murphy Biochem Exam 2 Questions and Answers
In the following figure, which bond would be unable to B (the bond close to the double bond)
rotate?
A
B
C
D
None of these choices
At pH 3, how many charged groups are present in the 4
penta peptide Ala-Asp-His-Ser-Lys
1
2
3
4
5
In chymotrypsin, only three amino acids are involved in The remaining amino acids serve all of these functions.
catalysis, but there are almost 200 amino acids in the
entire protein. What is
the function of the other amino acids?
Build the scaffold of the active site
stabilize the 3D structure of the active site
build the scaffold of potential regulatory sites
serve all these functions
None of the above
Proteins such as hemoglobin are known as _____ proteins allosteric
since binding of a molecule to one site alters binding to
other sites.
Ligand- activated
allosteric
induced -fit
cooperative
none of the above
While proteins are usually composed of linear chains of disulfide bonds
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
hydrogen bonds
glycosidic bonds
peptide bonds
disulfide bonds
ester linkages
Which of the following tripeptides would be expected to be GYA
the most hydrophobic?
KYG
DYG
DYA
KYA
GYA
The predominant non-covalent interaction seen in alpha- hydrogen bonds
helices and beta-sheets is ___.
electrostatic interactions
hydrogen bonds
dipole-dipole interaction
hydrophobic interactions
all of the above
, Rutgers Murphy Biochem Exam 2 Questions and Answers
The side chain of serine could interact with the side chain His; hydrogen bond
of ___ using a(n) ___.
Val; hydrophobic interaction
His; hydrogen bond
Gln; hydrophobic interaction
Asn; electrostatic interaction
none of the above
Myoglobin is _____; hemoglobin is _____. monomeric; tetrameric
monomeric; dimeric
dimeric; trimeric
monomeric; trimeric
dimeric; tetrameric
monomeric; tetrameric
Pancreatic lipase is necessary to break down fats in the Pancreatic lipase is an apoenzyme
body. It requires a protein, prolipase, to reach its peak
enzymatic activity. Which of the following statements is
most correct?
Pancreatic lipase is an apoenzyme
Prolipase is a vitamin
Prolipase is a prosthetic group
prolipase is a coenzyme
Which of the following amino acids is generally absent Pro
from an a helix?
Trp
Ser
Ile
Pro
none of the above
Which of the following best describes the peptide highly extended
backbone in a b sheet?
Coiled
compact
highly extended
rigid
None of the above
In a protein, the most conformationally restricted amino Pro, Gly
acid is __ ; the least conformationally restricted is __ .
Ile, Ala
Pro, Gly
Trp, Gly
Met, Cts
Ala, Pro
The two peptides shown in the diagram below are linked a disulfide bond ( bond between S-S atoms)
through
A hydrogen bond
a disulfide bond
a glycosidic bond
an ester linkage
a peptide bond
The average mass of an amino acid in a protein is 110 The molecular weight of the amino acids in titin are greater than 110 g/mol, because
g/mol. Dividing the mass of titin (3,816 kDa) by the number 110 g/mol represents an averaged
of amino acids molecular weight value obtained across several proteins having differing amino acid
(34,350) does not give the exact figure of 110. Why is this contents.
the case?
, Rutgers Murphy Biochem Exam 2 Questions and Answers
A protein has a predicted molecular weight of 47 kDa The protein is a dimer under native conditions.
based on the amino acid sequence, an apparent molecular
weight of 50 kDa by
SDS-PAGE, and an approximate molecular weight of 95
kDa by size exclusion chromatography. Each of these
techniques is described in
the appendix.
Size exclusion chromatography....
The protein is cleaved in half .....
That SDS-PAGE provides ....
The protein is a dimer under denaturing conditions.
The protein is a dimer under native conditions.
Lysine can form a salt bridge by interacting with the side Glu
chain of ___.
Pro
Ser
Glu
Gly
Asn
Which of the following atoms would be considered a A ( the one with NH)
hydrogen bond donor in a helix?
A
B
C
D
None of the above
The amino acid __ is commonly phosphorylated Ser/tyr
Ser/tyr
Asp
Asn
His
None of the above
Examine this enzyme structure. Where might you find the D (the little pocket within the enzyme)
active site on this enzyme?
A
B
C
D
On the reaction coordinate diagram shown below, A uncatalyzed
represents ___ reaction, B represents ___ reaction, and C catalyzed
is ___ G
Restriction enzymes are used in laboratory manipulations Enzymes are proteins and denature or unfold at higher temperatures
to cut DNA; many of these enzymes can be inactivated by
incubating them at 80 C for 30 minutes. Why do enzymes
not simply operate better at higher temperatures, as other
catalysts do?
Unable to lower Ea outside of their temperature range
other catalysts do not operate as efficiently at higher
temperature
Enzymes are proteins and denature or unfold at higher
temperatures
Need to be heated to much higher temperaturese to
improve...
In the following figure, which bond would be unable to B (the bond close to the double bond)
rotate?
A
B
C
D
None of these choices
At pH 3, how many charged groups are present in the 4
penta peptide Ala-Asp-His-Ser-Lys
1
2
3
4
5
In chymotrypsin, only three amino acids are involved in The remaining amino acids serve all of these functions.
catalysis, but there are almost 200 amino acids in the
entire protein. What is
the function of the other amino acids?
Build the scaffold of the active site
stabilize the 3D structure of the active site
build the scaffold of potential regulatory sites
serve all these functions
None of the above
Proteins such as hemoglobin are known as _____ proteins allosteric
since binding of a molecule to one site alters binding to
other sites.
Ligand- activated
allosteric
induced -fit
cooperative
none of the above
While proteins are usually composed of linear chains of disulfide bonds
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
hydrogen bonds
glycosidic bonds
peptide bonds
disulfide bonds
ester linkages
Which of the following tripeptides would be expected to be GYA
the most hydrophobic?
KYG
DYG
DYA
KYA
GYA
The predominant non-covalent interaction seen in alpha- hydrogen bonds
helices and beta-sheets is ___.
electrostatic interactions
hydrogen bonds
dipole-dipole interaction
hydrophobic interactions
all of the above
, Rutgers Murphy Biochem Exam 2 Questions and Answers
The side chain of serine could interact with the side chain His; hydrogen bond
of ___ using a(n) ___.
Val; hydrophobic interaction
His; hydrogen bond
Gln; hydrophobic interaction
Asn; electrostatic interaction
none of the above
Myoglobin is _____; hemoglobin is _____. monomeric; tetrameric
monomeric; dimeric
dimeric; trimeric
monomeric; trimeric
dimeric; tetrameric
monomeric; tetrameric
Pancreatic lipase is necessary to break down fats in the Pancreatic lipase is an apoenzyme
body. It requires a protein, prolipase, to reach its peak
enzymatic activity. Which of the following statements is
most correct?
Pancreatic lipase is an apoenzyme
Prolipase is a vitamin
Prolipase is a prosthetic group
prolipase is a coenzyme
Which of the following amino acids is generally absent Pro
from an a helix?
Trp
Ser
Ile
Pro
none of the above
Which of the following best describes the peptide highly extended
backbone in a b sheet?
Coiled
compact
highly extended
rigid
None of the above
In a protein, the most conformationally restricted amino Pro, Gly
acid is __ ; the least conformationally restricted is __ .
Ile, Ala
Pro, Gly
Trp, Gly
Met, Cts
Ala, Pro
The two peptides shown in the diagram below are linked a disulfide bond ( bond between S-S atoms)
through
A hydrogen bond
a disulfide bond
a glycosidic bond
an ester linkage
a peptide bond
The average mass of an amino acid in a protein is 110 The molecular weight of the amino acids in titin are greater than 110 g/mol, because
g/mol. Dividing the mass of titin (3,816 kDa) by the number 110 g/mol represents an averaged
of amino acids molecular weight value obtained across several proteins having differing amino acid
(34,350) does not give the exact figure of 110. Why is this contents.
the case?
, Rutgers Murphy Biochem Exam 2 Questions and Answers
A protein has a predicted molecular weight of 47 kDa The protein is a dimer under native conditions.
based on the amino acid sequence, an apparent molecular
weight of 50 kDa by
SDS-PAGE, and an approximate molecular weight of 95
kDa by size exclusion chromatography. Each of these
techniques is described in
the appendix.
Size exclusion chromatography....
The protein is cleaved in half .....
That SDS-PAGE provides ....
The protein is a dimer under denaturing conditions.
The protein is a dimer under native conditions.
Lysine can form a salt bridge by interacting with the side Glu
chain of ___.
Pro
Ser
Glu
Gly
Asn
Which of the following atoms would be considered a A ( the one with NH)
hydrogen bond donor in a helix?
A
B
C
D
None of the above
The amino acid __ is commonly phosphorylated Ser/tyr
Ser/tyr
Asp
Asn
His
None of the above
Examine this enzyme structure. Where might you find the D (the little pocket within the enzyme)
active site on this enzyme?
A
B
C
D
On the reaction coordinate diagram shown below, A uncatalyzed
represents ___ reaction, B represents ___ reaction, and C catalyzed
is ___ G
Restriction enzymes are used in laboratory manipulations Enzymes are proteins and denature or unfold at higher temperatures
to cut DNA; many of these enzymes can be inactivated by
incubating them at 80 C for 30 minutes. Why do enzymes
not simply operate better at higher temperatures, as other
catalysts do?
Unable to lower Ea outside of their temperature range
other catalysts do not operate as efficiently at higher
temperature
Enzymes are proteins and denature or unfold at higher
temperatures
Need to be heated to much higher temperaturese to
improve...
