Description
In this collection there will be a bunch of questions to help students review.
This collection will be useful for all chemistry, medical, pharmacy students
Study Set Content:
Questions with Answers- Proteins & Enzymes
A.
A peptide with 12 amino acids has the following amino acid composition:
2 Met, 1 Tyr, 1 Trp, 2 Glu, 1 Lys, 1 Arg, 1 Thr, 1 Asn, 1 Ile, 1 Cys
Reaction of the intact peptide with fluorodinitrobenzene followed by acid hydrolysis creates a
derivative of Ile.
A specific cleavage of the intact peptide produces fragments with the following sequences:
Glu-Cys-Asn-Met-Lys
Met-Glu-Thr-Arg-Trp
Ile-Tyr (Questions 1-5)
1._____ Which reagent was used for the specific cleavage?
a)
chymotrypsin
b)
trypsin
c)
V8 protease
d)
cyanogen bromide
2._____ Which amino acids would be released when the intact peptide was treated first with
V8 protease followed by treatment with cyanogen bromide?
a) Glu and Met
b)
Glu and Lys
c) Met and Lys
d) Glu, Met, and Lys
3._____
Which treatment would result in the release of Lys and Arg from the intact peptide?
a) trypsin
b) trypsin followed by dansyl chloride
c) trypsin followed by carboxypeptidase
d) trypsin followed by mild acid
4._____
If this intact peptide is sequenced using the Edman degradation, which step will
be part of the procedure?
a)
The Edman reagent will react with all 12 amino acids simultaneously.
b) Lithium borohydride will react with an
α
-carboxyl group.
c)
Phenylisothiocyanate will react with an
α
-amino group.
d)
Strong acid will be used to cleave off one modified amino acid.
5._____
If this peptide is normally part of a multimeric protein composed of four identical
subunits, what procedure might be needed prior to performing the Edman
degradation?
a)
The four subunits should be separated and sequenced individually.
b)
Two specific cleavages should be done to create two sets of fragments.
c)
Peptide bonds should be broken using hydrazine.
d)
Disulfide bonds should be reduced with mercaptoethanol.
______________________________________________________________________________
B.
A peptide has the following amino acid composition:
2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser
Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a
derivative of Met.
A specific cleavage of the intact peptide produces fragments with the following sequences:
Fragment A: Glu-Gly-Lys-Phe
Fragment B: Met-Ser-Leu-Arg
Fragment C: Met-Val-Glu-Phe (Questions 6-10)
6._____ Which reagent was used for the specific cleavage?
a) cyanogen bromide
b) V8 protease
c) chymotrypsin
d) trypsin
7._____
Which reagent would break only one peptide bond in the intact peptide?
a) cyanogen bromide
b) V8 protease
c) chymotrypsin
d) trypsin
8._____ Which amino acid would be released if the intact peptide was treated with a
combination of trypsin and chymotrypsin?
a) Lys
b) Phe
c) Glu
d) Met
9._____
What information do these result give about the sequence of the peptide?
a) The sequence is: Met-Val-Glu-Phe-Glu-Gly-Lys-Phe-Met-Ser-Leu-Arg
b) The sequence is: Met-Ser-Leu-Arg-Met-Val-Glu-Phe-Glu-Gly-Lys-Phe
c) The sequence is: Met-Val-Glu-Phe-Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe
d) The sequence is: Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe-Met Val-Glu-Phe
10._____
This peptide is one polypeptide chain of a multimeric protein that contains two
non-identical subunits. What problem might be seen when analyzing the primary
structure of the protein if the subunits were not separated?
a) Fluorodinitrobenzene
might
react
with two different amino acids.
b)
Carboxypeptidase might not react with the C-terminals.
c)
Mercaptoethanol might not reduce disulfide bonds.
d)
Lithium borohydride might cleave peptide bonds randomly.
_____________________________________________________________________________
C.
Protein A is an
α
-keratin while Protein B is a transport protein. (Questions 11-15)
11._____
Which characteristic could be shared by Protein A and Protein B?
a)
Both could be fibrous proteins containing multiple polypeptide chains.
b)
Both
could
be
globular
proteins with similar primary structures.
c)
Both could contain disulfide bridges linking methionine residues.
d)
Both could contain hydrogen bonds between peptide bond atoms.
12._____
When comparing Protein A to a
β
-keratin
a)
the
α
-keratin has a parallel structure while the
β
-keratin has an antiparallel
structure.
b) the
α
-keratin has a compact structure while the
β
-keratin has a more
extended structure.
c)
both have similar secondary structures that are low-energy states for the
proteins.
d) both contain hydroxyproline which functions as a prosthetic group.
13._____
When comparing Protein B to collagen,
a)
both are stabilized by van der Waals interactions.
b) both are stabilized by extensive regions of left-handed coils.
c)
both contain regions of random secondary structures.
d) both
contain
α
-helices as well as
β
-pleated sheets.
14._____
Which interaction is likely to occur in Protein B?
a)
A hydrophobic interaction could form between the R-groups of Val and
Leu.
b)
A hydrogen bond could form between the R-groups of Ser and Phe.
c)
A salt bridge could form between the R-groups of Arg and His.
d)
An ionic bond could form between the R-groups of Gln and Trp.
15._____ When comparing Protein A to Protein B,
a) both could be denatured by using heat to break amide bonds.
b) both could have primary structures that form with the help of chaperones.
c) both have conformations stabilized by numerous non-covalent bonds.
d) both contain the same proportions of hydrophilic and hydrophobic R-
groups.
D.
Protein A is a structural component while Protein B is an enzyme. The secondary structures
of both proteins are studied. (Questions 16-19)
16._____
Which could be characteristics of Protein A and Protein B?
a)
Protein A could have a low energy conformation while Protein B could
have a high energy conformation.
b)
Protein A could be a globular protein while Protein B could be a fibrous
protein.
c)
Protein A could contain mainly
α
-helix while Protein B could contain
equal amounts of
α
-helix and
β
-sheet.
d)
Protein A could be a type of collagen while Protein B could be a type of
keratin.
17._____
Which could be found within the structure of Protein B?
a)
A disulfide bond could form between two prosthetic groups.
b)
A salt bridge could form between two chaperones.
c)
Protein B could contain areas of random secondary structure stabilized by
van der Waals forces.
d)
Protein B could contain areas of repeating secondary structure stabilized
by hydrogen bonds.
18._____
Which is a characteristic of both an
α
-helix and a
β
-pleated sheet?
a)
Both can be anti-parallel structures.
b)
Both form interactions involving the oxygens of peptide bonds.
c) Both are found only within multimeric proteins.
d)
Both are denatured when heat breaks peptide bonds.
19._____
Which is a difference between an
α
-helix and a
β
-pleated sheet?
a)
An
α
-helix is a right-handed structure containing disulfide bonds while a
β
-pleated sheet is a left-handed structure containing ionic bonds.
b) An
α
-helix has a relatively extended spiral shape while a
β
-pleated sheet has
a relatively compact zig-zag shape.
c) An
α
-helix has non-covalent bonds between amino acids near each other
in the sequence while a
β
-pleated sheet has non-covalent bonds between
amino acids far apart in the sequence.
d)
An
α
-helix contains mainly amino acids with polar R-groups while a
β
-
pleated sheet contains mainly amino acids with non-polar R-groups.
_____________________________________________________________________________
E. Two proteins, myoglobin and hemoglobin, are compared. (Questions 20-30)
20._____
Which characteristics are shared by these two proteins?
a)
They both are globular proteins containing the common amino acids,
porphyrin, and iron.
b)
They both have closely related primary, secondary, tertiary, and
quaternary structures.
c)
They both are composed of multiple subunits each of which contains a
heme prosthetic group.
d)
They both have similar molecular weights and bind one oxygen molecule
per protein molecule.
21._____
Which is a property of protein tertiary structure?
a)
Tertiary structures usually contain hydrocarbon R-groups in the interior of
the protein where they can form hydrogen bonds.
b)
Tertiary structures usually contain hydroxyl R-groups on the exterior of
the protein where they can favorably interact with water.
c)
A protein’s tertiary structure can be predicted if the amino acid sequence is
known by performing the Edman degradation.
d)
A protein’s tertiary structure can be maintained by covalent salt bridges and
non-covalent disulfide bridges.
22._____
Which is a characteristic of protein quaternary structure?
a)
A protein composed of identical subunits has quaternary structure but not
tertiary structure.
b) A protein composed of non-identical subunits contains two polypeptide
chains with opposite charges.
c)
The quaternary structure of a multimeric protein always includes covalent
crosslinks between the subunits.
d)
The quaternary structure of a multimeric protein always depends upon the
primary structure of the subunits.
23._____
Which is a property of tertiary structure and quaternary structure?
a)
Both structures are stabilized by numerous covalent hydrophobic and
hydrophilic interactions.
b)
Both structures have specific shapes that depend upon the amino acid
sequence of the protein.
c)
Both structures form so that polar amino acid R-groups are found mainly in
the interior of the protein.
d)
Both structures must contain multiple
α
-helices and
β
-pleated sheets
connected by turns.
24._____
Which property is shared by both myoglobin and hemoglobin?
a)
Both are saturated with oxygen at low oxygen concentrations.
b)
Both display cooperative binding when transporting oxygen.
c)
Both contain strands of
β
-pleated sheet with a zig-zag shape.
d)
Both contain segments of
α
-helix with a spiral shape.
25._____
Which occurs when a hemoglobin molecule binds oxygen?
a)
Oxygen molecules in the lungs bind irreversibly to the protein’s heme
groups.
b)
The second oxygen molecule binds more easily than the first oxygen
molecule.
c)
The
α
subunits bind oxygen while the
β
subunits control cooperativity.
d)
Ionic bonds form between subunits which changes the quaternary structure.
26._____
Which change occurs when a hemoglobin subunit binds oxygen?
a)
A histidine residue changes position within the subunit.
b)
An iron atom is removed from a porphyrin group.
c)
The oxygen binds to amino acids within a segment of
α
-helix.
d) The oxygen causes a covalent crosslink to form within the subunit.
27._____
Which occurs when a hemoglobin molecule binds oxygen in the lungs?
a)
Each iron-porphyrin group can reversibly bind four oxygen molecules.
b)
Salt bridges between subunits break as the first oxygen binds.
c)
The first oxygen molecule binds more easily than the last oxygen molecule.
d)
Cooperative binding of oxygen causes the four subunits to dissociate.
28. _____ When myoglobin is denatured using heat
a) its amino acid composition will change.
b) its amino acid sequence will change.
c) its tertiary structure will change.
d) its C-terminal will change.
29._____
When hemoglobin is treated with urea and
β
-mercaptoethanol
a) its molecular weight will be unchanged.
b) its quaternary structure will be unchanged.
c) its primary structure will be unchanged.
d) its conformation will be unchanged.
30._____ Protein Z functions as an oxygen transport protein, and shares 60% of its primary
structure with myoglobin while the other 40% is different. Which is likely to be a
characteristic of Protein Z?
a) It probably contains one heme group that can bond two oxygen molecules.
b) It probably contains both
α
subunits and
β
subunits.
c) It probably could function even if a mutation changes one of the amino
acids in part of the primary structure that is shared with myoglobin.
d) It probably could function even if a mutation changes one of the amino
acids in part of the primary structure that is different from myoglobin.
_______________________________________________________________________________
F. Enzyme X and Enzyme Y are both involved in monosaccharide metabolism. Enzyme X uses
glucose as a substrate while Enzyme Y uses fructose as a substrate. At pH=7.0, Enzyme X
has a Vmax of 10
μ
M/s while Enzyme Y has a Vmax of 20
μ
M/s. Both enzymes have a K
M
of 3.0 mM for their respective substrates.(Questions 31-37)
31._____
Which aspects of its reaction will be changed by Enzyme Y?
a)
the activation energy of the reaction and the energy of the product
b)
the rate of the reaction and the energy of the transition state
c)
the equilibrium position of the reaction and the energy of the substrate
d)
the reversibility of the reaction and the energy of the active site
32._____ When its reaction is carried out at pH = 2.0, the Vmax of Enzyme X is 1.0
μ
M/s
because
a)
the enzyme is inhibited by its product at low pH.
b)
the enzyme is saturated with substrate at low pH.
c)
the enzyme is able to stabilize the transition state at low pH.
d)
the enzyme is partially denatured as R-groups protonate at low pH.
33._____
When the reaction is carried out at pH = 7.0 and the substrate concentration is
equal to the K
M
value
a)
X will produce more product than Y.
b)
Y will produce more product than X.
c)
X and Y will produce the same amount of product.
d)
X and Y will both work at their Vmax value.
34._____
Enzyme Y can also use the monosaccharide galactose as a substrate with a K
M
of
8.0 mM. Which will be a characteristic of Y as it binds galactose compared to its
binding to fructose?
a)
Y will form more non-covalent bonds with galactose.
b)
Y will form more covalent bonds with galactose.
c)
Y will have an active site that is less complementary to galactose.
d)
Y will undergo a greater conformational change as it binds galactose.
35._____ Which interaction is likely to occur as Enzyme X carries out its reaction?
a) A hydrogen bond could form between a serine R-group in the active site
and a carbonyl group in the transition state.
b)
An ionic bond could form between a glutamate R-group in the active site and
a carboxyl group in the substrate.
c)
A hydrophobic interaction could form between an asparagine R-group in the
active site and a methyl group in the substrate.
d)
A hydrogen bond could form between a valine R-group in the active site and
a hydroxyl group in the transition state.
36._____
Which kinetic property would Enzyme X display as it binds its normal substrate
and catalyzes its reaction?
a)
It could have an initial velocity independent of [S] when [S] < K
M
.
b)
It could have a K
M
value that decreases as [S] decreases from 3.0 mM to
0.3 mM.
c)
It could double the rate of its reaction as [S] increases from 3.0 mM to
30 mM.
d)
It could have a Vmax value that is dependent on [S] when [S] < K
M
.
37.______
Enzyme Y is allosterically inhibited by ribose and also inhibited by covalent
modification with phosphate. Which is a characteristic of its regulation?
a)
Y can covalently bind both ribose and phosphate to specific amino acids
within the protein.
b)
Y can establish an equilibrium with either ribose or phosphate to reduce
the activity of the enzyme.
c)
Y can bind both ribose and phosphate to a regulatory subunit with the help
of extra enzymes.
d)
Y can undergo reversible conformational changes when either ribose or
phosphate binds to the enzyme.
_____________________________________________________________________________
G.
The reactions of two enzymes, Enzyme A and Enzyme B, are studied at pH = 7.0. Both
enzymes produce glucose and have the same V
max
. Enzyme A has a K
M
of 2.0 mM while
Enzyme B has a K
M
of 5.0 mM. (Questions 38-44)
38. ______ Which characteristic will be shared by these two enzymes?
a) Both will increase the rate of their reaction by increasing the energy of the
substrate molecules.
b)
Both will properly orient the substrate for their reaction by forming
covalent bonds with the substrate.
c)
Both will decrease the activation energy of their reaction by being
complementary to the transition state.
d)
Both will shift the equilibrium of their reaction by lowering the energy
level of the product.
39. ______ Which property will Enzyme A likely have in common with most other
enzymes?
a) It can bind the substrate reversibly using specific amino acids.
b)
It can contain a dozen active sites each of which can bind a substrate
molecule.
c) It can undergo a small change in primary structure as the substrate binds.
d) It can be required in stoichiometric amounts in order to bind the correct
substrate.
40. ______ When Enzyme B carries out its reaction with a substrate concentration of 5.0
mM, the reaction velocity gradually decreases 5 minutes after the reaction starts.
What could cause this change in reaction rate?
a) Enzyme B catalyzes an irreversible reaction.
b) Enzyme B becomes saturated with substrate.
c) Enzyme B is inhibited by its product.
d) Enzyme B is working at its V
max
value.
41. ______ Which will occur when Enzyme A and Enzyme B both carry out their reaction at
pH = 7.0?
a) Enzyme A will produce more glucose than Enzyme B when [S] = 5.0 mM.
b) Enzyme B will produce more glucose than Enzyme A when [S] = 5.0 mM.
c) V
o
for Enzyme A will double as [S] increases from 5.0 mM to 10.0 mM.
d) V
o
for Enzyme B will double as [S] increases from 5.0 mM to 10.0 mM.
42. ______ Which kinetic property will be shared by Enzyme A and Enzyme B?
a) Their K
M
values will decrease as the substrate concentration decreases.
b) Their V
max
values will increase as the substrate concentration increases.
c) Their K
M
values will depend upon the concentration of the enzymes.
d) Their V
max
values will depend upon the slowest step of their reaction
mechanisms.
43. ______ The substrate for Enzyme A is a sugar phosphate while the substrate for Enzyme B
is a sugar alcohol. Which amino acid is likely to be found in the active site of both
enzymes?
a) leucine
b) tryptophan
c) aspartate
d) glutamine
44. ______ Enzyme A is an allosteric enzyme inhibited by galactose while Enzyme B is a
covalently modified enzyme inhibited by phosphate. Which will occur during their
regulation?
a)
Enzyme B will become more inhibited as the concentration of phosphate
increases.
b)
Enzyme A will become more inhibited as the concentration of galactose
increases.
c)
Both enzymes will undergo an irreversible conformational change as their
regulating molecule binds.
d)
Both enzymes will bind their regulating molecule to a specific active site
on a catalytic subunit.
_______________________________________________________________________________
