ANS: C PTS: 1 TOP: Protein Folding Dynamics 73.

The information
needed for the structure of a protein is contained in
a. amino acid composition
b. primary structure
c. secondary structure
d. tertiary structure
ANS: B PTS: 1 TOP: Protein Folding Dynamics 74. Incorrect protein
folding resulting in exposure of hydrophobic regions can result in
a. aggregation.
b. homology.
c. liposomes.
d. the Bohr effect.
ANS: A PTS: 1 OBJ: New in 6e TOP: Protein Folding Dynamics 75.
Proteins that aid in the correct and timely folding of other proteins are called
a. motifs.
b. chaperones.
c. liposomes.
d. cooperative.
ANS: B PTS: 1 TOP: Protein Folding Dynamics 76. The oxygen binding
curve of which of the following is the closest to that of myoglobin?
a. hemoglobin at pH 6.8
b. hemoglobin that lacks BPG
c. maternal hemoglobin
d. fetal hemoglobin
ANS: B PTS: 1 OBJ: New in 7e TOP: Protein Folding Dynamics 77.
The following amino acid causes a kink or bend in the α-helix.
a. Ala
b. Glu
c. Lys
d. Pro
e. Trp
Chapter 5—Protein Purification and Characterization Techniques MULTIPLE CHOICE 1.
What tends to happen to the percent recovery during a protein's purification?
a. The number usually steadily increases during the purification.
b. The number usually steadily decreases during the purification.
c. The number usually stays fairly constant during the purification.
d. There is no general trend for percent recovery during a protein purification.
ANS: B PTS: 1 OBJ: New in 6e TOP: Extracting Pure Proteins from Cells
2. Differential centrifugation at low speeds (several thousand RPM) is a
useful step when
a. organelles have been lysed.
b. enzymes of interest have different sizes.
c. cell membranes must be left intact.
d. ribosomes need to be broken down.
e. there are either organelles or debris to separate.
ANS: E PTS: 1 OBJ: Modified from 5e TOP: Extracting Pure Proteins
from Cells 3. The typical order for the major steps of enzyme isolation
would be (from first to last):
a. Homogenization, salt fractionation, electrophoresis, column chromatography.
b. Homogenization, column chromatography, salt fractionation, electrophoresis.
c. Homogenization, salt fractionation, column chromatography, electrophoresis.
 d. Salt fractionation, homogenization, electrophoresis, column chromatography.
e. Homogenization, electrophoresis, salt fractionation, column chromatography.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Extracting Pure Proteins
from Cells 4. The purity of an enzyme at various stages of purification is
best measured by
a. total protein.
b. total enzyme activity.
c. specific activity of the enzyme.
d. percent recovery of the protein.
e. percent recovery of the enzyme.
ANS: C PTS: 1 TOP: Extracting Pure Proteins from Cells 5. Salting out
with ammonium sulfate is based upon proteins interacting with other proteins via
a. hydrogen bonds.
b. ionic bonds.
c. hydrophobic interactions.
d. disulfide bonds.
ANS: C PTS: 1 TOP: Extracting Pure Proteins from Cells 6. Using
differential centrifugation it is possible to separate
a. nuclei, mitochondria, and ribosomes into three separate fractions
b. organelles from contaminating salts
c. proteins that differ in charge
d. proteins from membranes
ANS: A PTS: 1 TOP: Extracting Pure Proteins from Cells 7. The
following methods are useful for cell homogenization:
a. Sonication.
b. Freezing and thawing.
c. Detergents.
d. Enzymes.
e. All of these are correct.
ANS: E PTS: 1 TOP: Extracting Pure Proteins from Cells 8. Which of the
following happens as a protein is purified?
a. the percent recovery and the fold purification both increase
b. the percent recovery and the fold purification both decrease
c. the percent recovery increases and the fold purification decreases
d. the percent recovery decreases and the fold purification increases
ANS: D PTS: 1 TOP: Extracting Pure Proteins from Cells 9. Ammonium
sulfate is useful in protein purification because
a. it contains nitrogen and sulfur, both of which occur in proteins
b. it is sparingly soluble in water, causing proteins to co-precipitate with it
c. very pure proteins are obtained when it is used
d. it forms ion-dipole interactions with water, making proteins less soluble and more likely to
precipitate
ANS: D PTS: 1 TOP: Extracting Pure Proteins from Cells 10. The typical
order of differential centrifugation for organelles is (from slowest speed/lowest g to fastest speed/
highest g):
a. nuclei, microsomes, mitochondria & chloroplasts, cytosol, whole cells
b. whole cells, nuclei, mitochondria & chloroplasts, microsomes, cytosol
c. cytosol, microsomes, nuclei, mitochondria & chloroplasts, whole cells
d. nuclei, mitochondria & chloroplasts, whole cells, cytosol, microsomes
e. whole cells, cytosol, microsomes, nuclei, mitochondria & chloroplasts
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Extracting Pure Proteins
from Cells 11. Which of the following are principles on which to base
column chromatography?
a. Molecular size
b. Isoionic pH or pI
c. Ion exchange
d. Both molecular size and ion exchange
e. All of these
ANS: E PTS: 1 OBJ: Modified from 6e TOP: Column Chromatography
12. Which separates on the basis of molecular weight?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANS: A PTS: 1 TOP: Column Chromatography 13. Which separates
based on the ionic charge on a protein?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANS: E PTS: 1 TOP: Column Chromatography 14. Which type of
column is most affected by the shape of the protein, for example, comparing spherical and cigar-
shaped proteins?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANS: A PTS: 1 TOP: Column Chromatography 15. Which would be best
to separate a protein that binds strongly to its substrate?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANS: B PTS: 1 TOP: Column Chromatography 16. Elution of proteins
by means of a pH gradient would work best with this type of column:
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANS: E PTS: 1 TOP: Column Chromatography 17. Which would be best
to separate positively charged proteins?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANS: C PTS: 1 TOP: Column Chromatography 18. Which would be best
to separate proteins of similar size?
a. Gel filtration
b. Affinity chromatography
c. Cation exchange
d. Anion exchange
e. Cation or anion exchange
ANS: E PTS: 1 OBJ: Modified from 5e TOP: Column Chromatography
19. In affinity chromatography, a protein
a. which binds to the ligand will remain on the column.
b. which binds to the ligand will elute from the column.
c. which is hydrophobic will remain on the column.
d. which is hydrophilic will remain on the column.
ANS: A PTS: 1 TOP: Column Chromatography 20. In gel filtration
chromatography
a. materials are separated based on their size, the smaller ones eluting first.
b. materials are separated based on their size, the larger ones eluting first.
c. materials are separated based on their hydrophobic nature, the more hydrophobic ones
eluting first.
d. materials are separated based on their hydrophobic nature, the less hydrophobic ones
eluting first.
ANS: B PTS: 1 TOP: Column Chromatography 21. The order of elution
of AAs H, E, & K from a cation exchange column by a pH 6 buffer is
a. H E K
b. E H K
c. K H E
d. E K H
ANS: B PTS: 1 TOP: Column Chromatography 22. In any form of
chromatography, how will a compound which interacts more strongly with the stationary phase elute
compared to one that interacts less strongly?
a. A compound interacting more strongly will elute earlier than one with weaker interactions.
b. A compound interacting more strongly will elute later than one with weaker interactions.
c. The order of elution has nothing to do with interactions with the stationary phase, but with
interactions with the mobile phase.
ANS: B PTS: 1 OBJ: New in 6e TOP: Column Chromatography 23.
A chromatography technique where a solution of nonpolar compounds is put through a column
that has a nonpolar liquid immobilized on an inert matrix is which type of chromatography?
a. Gel filtration
b. Ion exchange
c. Affinity
d. HPLC
e. Reverse Phase HPLC
ANS: E PTS: 1 OBJ: New in 7e TOP: Column Chromatography 24.
In a sample consisting of lysine, leucine, and glutamic acid, which will be eluted last from an
anion exchange resin at pH 7?
a. all three will be eluted at the same time
b. lysine
c. leucine
d. glutamic acid
ANS: D PTS: 1 OBJ: Modified from 5e TOP: Column Chromatography
25. In chromatography the experimental setup always requires
a. a stationary phase and a mobile phase
b. a spectrophotometric detecting device
 c. a sample in which components differ in charge
d. a sample in which components differ in polarity
ANS: A PTS: 1 TOP: Column Chromatography 26. A separation of a
mixture of cations of different charge requires
a. another cationic substance
b. an anionic substance
c. an electrically neutral, but highly polar, substance
d. an electrically neutral, nonpolar substance
ANS: B PTS: 1 TOP: Column Chromatography 27. Which of the
following is not an example of column chromatography?
a. ammonium sulfate fractionation
b. ion-exchange separation
c. HPLC
d. affinity separation
ANS: A PTS: 1 TOP: Column Chromatography 28. In affinity chro-
matography
a. there is nonspecific binding of proteins to column material
b. only minor purifications can be obtained
c. the mobile phase is always pure water
d. the ligand is alwayse specific for one type of protein to be bound
e. there can be molecule specific ligands or group specific ligands
ANS: E PTS: 1 OBJ: Modified from 6e TOP: Column Chromatography
29. The degree of separation in molecular sieve chromatography depends on
a. the polarity of the mobile phase
b. the pKa of the buffer material in the mobile phase
c. the chemical nature of the sieve material
d. the size of the pores in the sieve material
ANS: D PTS: 1 TOP: Column Chromatography 30. In all forms of
chromatography one way of identifying eluted substances is by
a. fluorescence spectroscopy
b. comparison with standards
c. radioactive labeling
d. treating fractions with a reagent that will cause a color change
ANS: B PTS: 1 TOP: Column Chromatography 31. Which substance
would you expect to be eluted first from a molecular sieve column with a suitable degree of crosslink-
ing?
a. hemoglobin
b. myoglobin
c. 2,3-bisphosphoglycerate
d. all would elute at the same rate
ANS: A PTS: 1 TOP: Column Chromatography 32. In the SDS-PAGE
(sodium dodecylsulfate - polyacrylamide gel electrophoresis) method, separation takes place on the
basis of
a. charge only, because all particles have different charges, but the same mass.
b. the sieving action of the gel, because all particles have the same charge, but different
masses.
c. the sieving action of the gel, because all particles have approximately the same charge/mass
ratio, but different masses.
d. the chemical nature of the buffer used as the electrolyte.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Electrophoresis 33.
How many bands would be produced when hemoglobin is subjected to SDS-PAGE?
 a. 1
b. 2
c. 3
d. 4
e. 2, but only if the size of the pores in the gel would allow two proteins of slightly different
size to be separated
ANS: E PTS: 1 OBJ: Modified in 7e TOP: Electrophoresis 34.
The following are all principles on which to base electrophoresis except:
a. Molecular size
b. Isoionic pH or pI
c. Net charge
d. Binding to a substrate
e. Shape
ANS: D PTS: 1 TOP: Electrophoresis 35. Two-dimensional elec-
trophoresis usually exploits these 2 different properties of proteins:
a. Molecular weight and shape
b. Molecular weight and net charge
c. Molecular weight and isoionic pH
d. Isoionic pH and shape
e. Isoionic pH and net charge
ANS: B PTS: 1 TOP: Electrophoresis NARRBEGIN: Exhibit 5A Exhibit 5A The
following diagram shows the anode, cathode, and pH gradient of an isoelectric focusing bed:
anode+ −cathode
pH 1 2 3 4 5 6 7 8 9 10 11 12 13 14
NARREND 36. Refer to Exhibit 5A. If the amino acid glycine were placed in the bed where
the pH is 7, and the current were turned on, it would migrate closest to which of the following
positions?
a. pH 4
b. pH 6
c. pH 8
d. pH 10
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Electrophoresis 37.
Refer to Exhibit 5A. If the amino acid glycine were placed in the bed where the pH is 11, and
the current were turned on, it would migrate closest to which of the following positions?
a. pH 4
b. pH 6
c. pH 8
d. pH 10
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Electrophoresis 38.
Refer to Exhibit 5A. A mixture of asp, asn, and arg is placed in the bed where the pH is 7, and
the current is turned on. From left to right, which best represents the final positions of the individual
amino acids?
a. asp asn arg
b. arg asn asp
c. asn asp arg
d. arg asp asn
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Electrophoresis 39.
When electrophoretic separations are done based on molecular weight, the distance that a
molecule moves can be graphed as a straight line when compared to:
a. the MW of the proteins
b. the negative of the MW of the proteins
 c. the log of the MW of the proteins
d. none of these
ANS: C PTS: 1 OBJ: New in 7e TOP: Electrophoresis 40. In elec-
trophoresis experiments
a. the separation must be carried out in bright light
b. the polarity of substances to be separated is more important than their charge or size
c. the sample can be badly degraded as a result of the separation
d. an electric field must be applied to the mixture to be separated
ANS: D PTS: 1 TOP: Electrophoresis 41. In isoelectric focusing gel
electrophoresis
a. particular care must be taken to ensure the same pH along the length of the gel
b. there is a pH gradient that parallels the electric field gradient
c. the electric current is allowed to fluctuate
d. the electric circuits of the apparatus must be very well insulated
ANS: B PTS: 1 TOP: Electrophoresis 42. The isoelectric point is
a. the pH at which a substance has no net charge
b. the pH at which a substance has a net positive charge
c. the pH at which a substance has a net negative charge
d. the pH at which a substance has no charge groups of any kind
ANS: A PTS: 1 TOP: Electrophoresis 43. Two dimensional separation
methods
a. lead to unreliable results
b. are not widely used because of their complexity
c. do not improve separation
d. consist of two separation methods applied in sequence
ANS: D PTS: 1 TOP: Electrophoresis 44. Important steps in sequenc-
ing pure proteins include all of these except:
a. Determining the amino acid composition
b. Determining the isoionic pH of the protein
c. Breaking the protein into smaller peptides
d. Determining the amino acids on the ends of the protein
e. Determining the amino acids on the ends of the smaller peptides
ANS: B PTS: 1 TOP: Primary Structure Determination 45. If a protein
with the sequence FEWPRQVDMARINE is treated with chymotrypsin, what will the products be?
a. F EW PRQVMARINE
b. FE WPRQVD MARINE
c. FEWPR QVDMAR INE
d. FEWPRQVDM ARINE
ANS: A PTS: 1 OBJ: New in 6e TOP: Primary Structure Determination
46. Which of the following treatments results in a polypeptide fragment with a homoser-
ine lactone at the C-terminal end?
a. trypsin
b. chymotrypsin
c. cyanogen bromide
d. Edman method
ANS: C PTS: 1 OBJ: New in 6e TOP: Primary Structure Determination
47. If a protein with the sequence PQRKYPIG is treated with trypsin, what will the
products be?
a. PQR KYPIG
b. PQRK YPIG
c. PQR K YPIG
 d. PQ R KPIG0
ANS: C PTS: 1 TOP: Primary Structure Determination 48. Cyanogen
bromide (CNBr) cleaves proteins
a. after positively charged residues, such as K & R.
b. after negatively charged residues, such as D & E.
c. after aromatic residues, such as Y & W.
d. after methionine residues.
ANS: D PTS: 1 TOP: Primary Structure Determination 49. It is
impossible to sequence a protein if you do not have overlapping sequences to work with.
a. True
b. False
ANS: B PTS: 1 TOP: Primary Structure Determination 50. The most
efficient method for determining the sequence of a short peptide is:
a. Edman degradation
b. Trypsin digestion
c. Chymotrypsin digestion
d. Cyanogen bromide digestion
ANS: A PTS: 1 OBJ: Modified in 7e TOP: Primary Structure Determi-
nation 51. Methods for breaking proteins into smaller peptides include all of the following
except:
a. Digestion with chymotrypsin
b. Cyanogen Bromide treatment
c. Digestion with Trypsin
d. Edmann degradation
e. All of the above create short peptides suitable for sequencing
ANS: D PTS: 1 TOP: Primary Structure Determination 52. When end-
group analysis was done on the protein insulin, the results indicated that both glycine and phenyl-
alanine were N-terminal amino acids and both asparagine and alanine were C-terminal amino acids.
These results indicate that
a. the experiment was done incorrectly
b. no conclusions can be drawn
c. there were impurities in the sample
d. insulin consists of two polypeptide chains
ANS: D PTS: 1 TOP: Primary Structure Determination 53. Matrix-
Assisted Laser Desorption Ionization is a type of _______ technique.
a. electrophoresis
b. ion exchange chromatography
c. affinity chromatography
d. mass spectrometry
ANS: D PTS: 1 OBJ: New in 7e TOP: Primary Structure Determination
54. An amino acid analyzer is an instrument used to determine
a. the sequence of amino acids in a polypeptide chain
b. the identity of N-terminal and C-terminal amino acids in a protein
c. the presence of modified amino acids in a protein
d. the identities and relative amounts of amino acids in a protein
ANS: D PTS: 1 TOP: Primary Structure Determination 55. Generally
speaking, sequence techniques have become so sensitive that if you are able to isolate the protein on a
gel, there is enough of it to get a significant amount of its sequence.
a. True
b. False
ANS: A PTS: 1 TOP: Primary Structure Determination 56. Determina-
tion of the sequence of amino acids in a peptide is done by
 a. x-ray crystallography
b. Edman degradation
c. treatment with cyanogen bromide
d. trypsin hydrolysis
ANS: B PTS: 1 TOP: Primary Structure Determination 57. It is
frequently possible to bypass the determination of the identity of the N-terminal amino acid of a
protein because
a. this information is already available from the amino acid analysis
b. the Edman method sequences the peptide from the N-terminal end
c. N-terminal amino acids are always chemically modified
d. this information is not needed
ANS: B PTS: 1 TOP: Primary Structure Determination 58. Which of the
following is not used in protein structure determination?
a. digestion with proteolytic enzymes
b. the Edman method
c. treatment with cyanogen bromide
d. treatment with alkyl halides
ANS: D PTS: 1 TOP: Primary Structure Determination Chapter 6—The Behavior
of Proteins: Enzymes MULTIPLE CHOICE 1. How much faster is a reaction with the fastest
enzyme than without a catalyst?
a. About 10 times faster.
b. About 100 times faster.
c. About 1,000 times faster.
d. About 10,000 times faster.
e. About 1020 times faster.
ANS: E PTS: 1 OBJ: Modified from 5e TOP: Enzymes Are Effective
Biological Catalysts 2. As catalysts, enzymes are
a. significantly less effective than nonenzymatic catalysts
b. slightly less effective than nonenzymatic catalysts
c. significantly more effective than nonenzymatic catalysts
d. slightly more effective than nonenzymatic catalysts
ANS: C PTS: 1 TOP: Enzymes Are Effective Biological Catalysts 3. The
rate of a reaction depends on
a. the free energy change
b. the activation energy
c. the enthalpy change
d. the entropy change
ANS: B PTS: 1 TOP: Kinetics Versus Thermodynamics 4. Enzymatic
activity has an optimum temperature because
a. the component amino acids have varying melting points
b. the rate of reactions is thermodynamically controlled
c. the side chains of essential residues are chemically degraded at higher temperatures
d. raising the temperature speeds up the reaction until protein denaturation sets in
ANS: D PTS: 1 TOP: Kinetics Versus Thermodynamics 5. The main
difference between a catalyzed and an uncatalyzed reaction is that
a. the activation energy of the catalyzed reaction is lower.
b. the catalyzed reaction has a more favorable free energy change.
c. the catalyzed reaction has a more favorable enthalpy change.
d. the catalyzed reaction has a more favorable entropy change.
ANS: A PTS: 1 TOP: Kinetics Versus Thermodynamics 6. Which of the
following is not true?
 a. In thermodynamics, spontaneous does not mean instantaneous or even fast.
b. If a reaction is spontaneous then it has a negative ΔG.
c. Speed of a reaction is a kinetic parameter, not a thermodynamic one.
d. A reaction with a positive ΔG0 can never happen
ANS: D PTS: 1 OBJ: New in 7e TOP: Kinetics Versus Thermodynamics
7. What effect does a catalyst have on the ΔG° of a reaction?
a. A catalyst lowers the ΔG°.
b. A catalyst raises the ΔG°.
c. A catalyst has no effect on the ΔG°.
d. It depend on the specific catalyst.
ANS: C PTS: 1 OBJ: New in 6e TOP: Kinetics Versus Thermodynamics
8. Which of the following is most directly related to the speed of a reaction?
a. The temperature
b. The ΔG0 of the reaction
c. The ΔG of the reaction
d. The ΔG0‡ of the reaction
e. None of these is correct.
ANS: D PTS: 1 OBJ: New in 7e TOP: Kinetics Versus Thermodynamics
9. A rate constant is
a. the rate of a reaction at standard temperature and pressure.
b. the rate of a reaction at equilibrium.
c. a proportionality constant relating the rate of a reaction to the concentration(s) of the
reactant(s).
d. a kind of transition state.
ANS: C PTS: 1 OBJ: New in 6e TOP: Kinetics Versus Thermodynamics
10. The rate of a reaction is always dependent on the concentration(s) of the reactant(s).
a. True
b. False
ANS: B PTS: 1 OBJ: New in 6e TOP: Kinetics Versus Thermodynamics
11. All catalysts work by lowering the activation energy for a reaction.
a. True
b. False
ANS: A PTS: 1 TOP: Kinetics Versus Thermodynamics 12. The amount
of energy released during a reaction tells nothing about the rate at which that reaction will occur.
a. True
b. False
ANS: A PTS: 1 TOP: Kinetics Versus Thermodynamics 13. Thermody-
namically favorable reactions all release energy.
a. True
b. False
ANS: A PTS: 1 TOP: Kinetics Versus Thermodynamics 14. The sign of
Gibb's Free Energy is positive ("+") when energy is released.
a. True
b. False
ANS: B PTS: 1 TOP: Kinetics Versus Thermodynamics 15. The order of
a reaction can be determined from the balanced equation for the reaction.
a. True
b. False
ANS: B PTS: 1 TOP: Kinetics Versus Thermodynamics 16. The kinetic
order of a reaction
 a. can be determined by inspection from the coefficients of the balanced equation
b. must be determined experimentally
c. always depends on the concentration of enzyme
d. never depends on concentrations of reactants
ANS: B PTS: 1 TOP: Kinetics Versus Thermodynamics 17. Given the
rate law, rate = k[A][B], the overall reaction order is
a. zero
b. one
c. two
d. cannot be determined
ANS: C PTS: 1 TOP: Kinetics Versus Thermodynamics 18. First order
kinetics means:
a. The rate of a reaction is independent of the amount of reactant measured.
b. The rate of the reaction varies directly with the amount of reactant measured.
c. The rate of the reaction varies with the square of the amount of the reactant measured.
d. More information is needed to answer this question.
e. None of these is correct.
ANS: B PTS: 1 TOP: Kinetics Versus Thermodynamics 19. The active
site of an enzyme
a. is frequently located in a cleft in the enzyme.
b. is the portion of the enzyme to which the substrate binds.
c. contains the reactive groups that catalyze the reaction.
d. all of these
ANS: D PTS: 1 OBJ: Modified in 7e TOP: Enzyme-Substrate Binding
20. A transition state analogue
a. binds tightly to the enzyme
b. enhances the activity of the enzyme when bound to it
c. forms a complex with the enzyme that is energetically stable compared to the enzyme-
substrate complex
d. will bind to the enzyme by the lock-and-key mechanism rather than the induced-fit
mechanism
ANS: A PTS: 1 TOP: Enzyme-Substrate Binding 21. The substrate will
only bind to the enzyme when the shapes fit together rigidly.
a. True
b. False
ANS: B PTS: 1 TOP: Enzyme-Substrate Binding 22. In the induced-fit
model of substrate binding to enzymes
a. the substrate changes its conformation to fit the active site
b. the active site changes its conformation to fit the substrate
c. there is a conformational change in the enzyme when the substrate binds
d. there is aggregation of several enzyme molecules when the substrate binds
ANS: C PTS: 1 TOP: Enzyme-Substrate Binding 23. The E-S complex
often shows as a slight depression in the energy profile for the reaction.
a. True
b. False
ANS: A PTS: 1 TOP: Enzyme-Substrate Binding 24. The active site of an
enzyme is the place where the following happens:
a. The enzyme substrate complex forms here.
b. The catalytic reaction happens here.
c. Allosteric regulation of enzyme rate occurs here.
d. The enzyme-substrate complex forms and the reaction occurs at the active site.
 e. All of these are correct.
ANS: D PTS: 1 TOP: Enzyme-Substrate Binding 25. Which of the
following is implied by induced fit between the enzyme's active site and the substrate?
a. The enzyme is a flexible molecule.
b. An enzyme will work equally well with different substrates.
c. An active site can bind to different substrates.
d. The enzyme is a flexible molecule so different substrates can bind.
e. All of these
ANS: E PTS: 1 OBJ: Modified from 6e TOP: Enzyme-Substrate Binding
26. Which of the following is true?
a. The E-S complex often dissociates with no reaction taking place.
b. The E-S complex must form before a reaction can take place
c. Once the E-S complex forms, it can go on to form product or dissociate to E + S
d. All of these
ANS: D PTS: 1 OBJ: New in 7e TOP: Enzyme-Substrate Binding 27.
Which of the following is true about the enzyme chymotrypsin?
a. The enzyme can cleave peptides.
b. The enzyme can cleave esters.
c. The enzyme only binds to aromatic substrates.
d. The enzyme can cleave substrates which are not naturally occurring.
e. All of these are true.
ANS: E PTS: 1 OBJ: Modified from 5e TOP: Examples of Enzyme-
Catalyzed Reactions 28. The reaction catalyzed by aspartate transcarbamoylase is
a. the first step in the synthesis of amino acids.
b. the first step in the synthesis of fatty acids.
c. the first step in the synthesis of CTP and UTP.
d. is part of glycolysis.
ANS: C PTS: 1 OBJ: New in 6e TOP: Examples of Enzyme-Catalyzed
Reactions 29. In the reaction catalyzed by chymotrypsin, a graph in which the rate is
plotted against the concentration of substrate
a. is sigmoidal, characteristic of an allosteric enzyme
b. shows that cooperative kinetics are observed
c. shows that the reaction is zero order
d. is hyperbolic, characteristic of a nonallosteric enzyme
ANS: D PTS: 1 TOP: Examples of Enzyme-Catalyzed Reactions 30. In
the reaction catalyzed by aspartate transcarbamoylase, a graph in which the rate is plotted against the
concentration of substrate
a. is sigmoidal, characteristic of an allosteric enzyme
b. shows that noncooperative kinetics are observed
c. shows that the reaction is zero order
d. is hyperbolic, characteristic of a nonallosteric enzyme
ANS: A PTS: 1 TOP: Examples of Enzyme-Catalyzed Reactions 31.
Which of the following describes the unique importance of protein Kinase Mζ (PKMζ)?
a. It is a protein kinase
b. It uses ATP to phosphorylate a substrate
c. It is an allosteric enzyme
d. It has been implicated in the formation of long-term memories
ANS: D PTS: 1 OBJ: New in 7e TOP: Examples of Enzyme-Catalyzed
Reactions 32. The Michaelis-Menten approach to describing the kinetics of an
enzyme-catalyzed reaction makes which of the following assumptions about the conversion of product
into substrate?
a. The product binds reversibly to the enzyme in order to be converted into the substrate.
b. The product is not converted to substrate to any appreciable extent.
c. The product is converted to substrate following simple first order kinetics.
d. The product is converted to substrate following simple second order kinetics.
ANS: B PTS: 1 OBJ: Modified from 6e TOP: Michaelis-Menten Approach
33. The initial rate of an enzymatic reaction is usually determined in order to assure that
a. the enzyme is active
b. there is no reverse reaction of product to the enzyme-substrate complex
c. the substrate is not used up
d. the experiment can be completed quickly
ANS: B PTS: 1 TOP: Michaelis-Menten Approach 34. According to the
steady-state assumption
a. the product concentration does not change significantly
b. the substrate concentration is large and does not change significantly
c. the concentration of enzyme-substrate complex remains constant with time
d. the free enzyme concentration is always in great excess to the concentration of enzyme-
substrate complex
ANS: C PTS: 1 TOP: Michaelis-Menten Approach 35. Most enzyme
reactions display first order kinetics for the individual substrates when the substrate concentration is
low.
a. True
b. False
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Michaelis-Menten Approach
36. When the substrate concentration is low, an enzyme reaction
a. will display zero-order kinetics.
b. will display first-order kinetics.
c. will display second-order kinetics.
d. will denature and cease to function.
ANS: B PTS: 1 OBJ: New in 6e TOP: Michaelis-Menten Approach 37.
When an enzyme is saturated with substrates,
a. it will display zero-order kinetics.
b. it will display first-order kinetics.
c. it will display second-order kinetics.
d. it will denature and cease to function.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Michaelis-Menten Approach
38. The Michaelis constant is
a. related to the molecular weight of the enzyme
b. a measure of the resistance of the enzyme to denaturation
c. a reflection of the percentage of polar amino acids in the enzyme
d. a measure of how tightly the substrate is bound to the enzyme
ANS: D PTS: 1 TOP: Michaelis-Menten Approach 39. The KM expression
is equal to
a. (k1 + k2) / k−1
b. (k−1 + k2) / k1
c. (k1 + k−1) / k2
d. k−1 / k1
ANS: B PTS: 1 TOP: Michaelis-Menten Approach 40. Which of the
following are related for a given enzyme?
a. Vmax, KM, and percentage of α-helix
 b. Vmax, kcat, and percentage of β-sheet
c. Vmax, kcat, and turnover number
d. Vmax, KM, and molecular weight
ANS: C PTS: 1 TOP: Michaelis-Menten Approach 41. The Michaelis
constant is
a. the rate constant for the formation of the substrate-enzyme (E-S) complex.
b. the rate constant for the breakdown of the substrate-enzyme (E-S) complex to form free
enzyme and substrate.
c. the rate constant for the breakdown of the substrate-enzyme (E-S) complex to form free
enzyme and product.
d. a compilation of several rate constants for the reaction.
ANS: D PTS: 1 OBJ: Modified from 5e TOP: Michaelis-Menten Approach
42. The drug acetazolamide:
a. Is used to help fight altitude sickness
b. Was found to ruin the taste of carbonated beverages
c. Does not affect the taste of non-carbonated liquors
d. Causes its effect on taste by inhibiting carbonic anhydrase 4
e. All of these
ANS: E PTS: 1 OBJ: New in 7e TOP: Michaelis-Menten Approach 43.
The substrate-enzyme (E-S) complex
a. always proceeds to form the products rapidly.
b. always breaks down to form free enzyme and substrate.
c. always breaks down to form free enzyme and product.
d. may break down to form free enzyme and substrate, or free enzyme and product.
ANS: D PTS: 1 OBJ: Modified from 5e TOP: Michaelis-Menten Approach
44. A Lineweaver-Burk plot is useful in the analysis of enzymatic reactions because
a. it is easier to see whether points deviate from a straight line than from a curve
b. it is not affected by the presence of inhibitors
c. it can be used whether or not the enzyme displays Michaelis-Menten kinetics
d. all of the above
ANS: A PTS: 1 TOP: Michaelis-Menten Approach 45. The steady state of
an enzyme reaction is the following:
a. The rate observed just after mixing the enzyme and substrate.
b. The rate observed and Vmax.
c. The rate of product formation.
d. The state which exists when E-S complex is forming as fast as it is breaking down.
e. The state which exists when substrate concentration equals KM.
ANS: D PTS: 1 TOP: Michaelis-Menten Approach 46. If the y-intercept of a
Lineweaver-Burk plot = 1.91 (sec/millimole) and the slope = 75.3 L/sec, Vmax equals:
a. 0.0254 millimoles per second.
b. 0.523 millimoles per second.
c. 5.23 millimoles per second.
d. 39.4 millimoles per second.
e. 75.3 millimoles per second.
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Michaelis-Menten Approach
47. If the y-intercept of a Lineweaver-Burk plot = 1.91 (sec/millimole) and the slope =
75.3 L/sec, KM equals:
a. 0.0254 millimolar (mM).
b. 0.523 millimolar (mM).
c. 5.23 millimolar (mM).
d. 39.4 millimolar (mM).
e. 75.3 millimolar (mM).
ANS: D PTS: 1 OBJ: Modified from 5e TOP: Michaelis-Menten Approach
48. The Michaelis constant determines the Vmax of an enzymatic reaction.
a. True
b. False
ANS: B PTS: 1 TOP: Michaelis-Menten Approach 49. It is important that at
physiological conditions, enzymes work at Vmax.
a. True
b. False
ANS: B PTS: 1 TOP: Michaelis-Menten Approach NARRBEGIN: Exhibit 6A
Exhibit 6A This is a reaction going on in your muscle cells right this very minute: The enzyme triose
phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway.
It follows simple Michaelis-Menten kinetics: Typical cellular concentrations: triose phosphate
isomerase = 0.1 nM dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM
NARREND 50. Refer to Exhibit 6A. What is the equilibrium constant for the uncatalyzed
reaction?
a. 0.9
b. 1.1
c. 2.5
d. Cannot be determined from the information provided.
ANS: A PTS: 1 TOP: Michaelis-Menten Approach 51. Refer to Exhibit
6A. What is the KM of the enzyme?
a. 10 nM
b. 0.1 µM
c. 1 µM
d. 10 µM
ANS: D PTS: 1 TOP: Michaelis-Menten Approach 52. Refer to Exhibit
6A. What is the Vmax of the enzyme?
a. 90 nM/s
b. 4500 µM/s
c. 200 µM/s
d. 0.5 M/s
ANS: A PTS: 1 TOP: Michaelis-Menten Approach 53. Refer to Exhibit
6A. What is the actual velocity of the forward reaction under physiologic conditions?
a. 2 nM/s
b. 45 nM/s
c. 500 nM/s
d. 30 nM/s
ANS: D PTS: 1 TOP: Michaelis-Menten Approach 54. Refer to Exhibit
6A. What is the equilibrium constant for the enzyme-catalyzed reaction?
a. 0.9
b. 1.1
c. 2.5
d. Cannot be determined from the information provided.
ANS: A PTS: 1 TOP: Michaelis-Menten Approach 55. Refer to Exhibit
6A. "Restrainin" is an inhibitor of triose phosphate isomerase. When it is added to cells at a concentra-
tion of 0.4 nM, the enzyme's apparent KM for the substrate is altered to 100 µM, but the Vmax is
unchanged.
a. This is a competitive inhibitor.
b. This is an uncompetitive inhibitor.
c. This is a noncompetitive inhibitor.
d. This is an irreversible inhibitor.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Enzyme Inhibition
56. Refer to Exhibit 6A. "Restrainin" is an inhibitor of triose phosphate isomerase. When
it is added to cells at a concentration of 0.4 nM, the enzyme's apparent KM for the substrate is altered
to 100 µM, but the Vmax is unchanged. In the following graph, which line best represents the
Lineweaver-Burk plot obtained in the presence of restrainin?
a. A
b. B
c. C
d. D
e. E
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Enzyme Inhibition
57. Refer to Exhibit 6A. "Hindrate" is an inhibitor of triose phosphate isomerase. When it
is added to cells at a concentration of 0.1 nM, the enzyme's KM for the substrate is unchanged, but the
apparent Vmax is altered to 50 nM/sec.
a. This is a competitive inhibitor.
b. This is an uncompetitive inhibitor.
c. This is a noncompetitive inhibitor.
d. This is an irreversible inhibitor.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Enzyme Inhibition
58. Refer to Exhibit 6A. "Hindrate" is an inhibitor of triose phosphate isomerase. When it
is added to cells at a concentration of 0.1 nM, the enzyme's KM for the substrate is unchanged, but the
apparent Vmax is altered to 50 nM/sec. In the following graph, which line best represents the
Lineweaver-Burk plot obtained in the presence of hindrate?
a. A
b. B
c. C
d. D
e. E
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Enzyme Inhibition
59. Which of the following statements regarding the Michaelis constant is false?
a. It is similar to the affinity constant between the enzyme and substrate.
b. The dimension for the Michaelis constant is concentration, such as molarity.
c. The Michaelis constant determines the Vmax.
d. It is the substrate concentration necessary to reach 1/2 Vmax.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Michaelis-Menten Approach
60. To study the nature of an enzyme, Vmax is not as good a measurement as the catalytic
rate constant kcat because:
a. The Vmax is not a true constant since it depends on the concentration of enzyme
b. The Vmax cannot be measured
c. The Vmax is only valid for allosteric enzymes
d. none of these
ANS: A PTS: 1 OBJ: New in 7e TOP: Michaelis-Menten Approach 61.
The KM of hexokinase for glucose = 0.15 mM and for fructose, KM = 1.5 mM. Which is the
preferred substrate?
 a. Glucose.
b. Fructose.
c. Neither substrate is preferred over the other.
d. You cannot tell from the data given.
e. None of these answers is correct.
ANS: A PTS: 1 TOP: Michaelis-Menten Approach 62. Competitive
inhibitors have this effect:
a. Modifying the KM value.
b. Changing the value for Vmax.
c. Interfering with substrate binding.
d. This type of inhibitor both changes the KM and interferes with substrate binding.
e. All of these are correct.
ANS: D PTS: 1 TOP: Enzyme Inhibition 63. Which of the
following inhibitors binds to the enzyme at a site other than the active site?
a. competitive inhibitor
b. noncompetitive inhibitor
c. irreversible inhibitor
d. all of these
e. none of these
ANS: B PTS: 1 OBJ: Modified from 6e TOP: Enzyme Inhibition
64. Inhibitors can have the following effects on enzyme kinetics:
a. Modifying the KM value.
b. Changing the value for Vmax.
c. Interfering with substrate binding.
d. An inhibitor can change the KM and interfere with substrate binding.
e. All of these are correct.
ANS: E PTS: 1 TOP: Enzyme Inhibition 65. The value of Vmax
changes in
a. competitive inhibition
b. noncompetitive inhibition
c. both forms of inhibition
d. neither form of inhibition
ANS: B PTS: 1 TOP: Enzyme Inhibition 66. The fundamental
difference between competitive and noncompetitive inhibition is
a. the degree of cooperativity of the reaction
b. the size of the active site of the enzyme
c. the manner of binding of substrate to the enzyme
d. the manner of binding of inhibitor to the enzyme
ANS: D PTS: 1 TOP: Enzyme Inhibition 67. Which of the
following is more likely to inhibit regulatory subunits of an allosteric enzyme?
a. A competitive inhibitor
b. A non-competitive inhibitor
c. An irreversible inhibitor
d. All of these are equally likely to inhibit a regulatory subunit
ANS: B PTS: 1 OBJ: New in 7e TOP: Enzyme Inhibition 68. For
competitive inhibition
a. the value of KM decreases
b. the value of Vmax decreases
 c. it is possible to overcome the effect of the inhibitor by increasing the concentration of
substrate
d. none of the above
ANS: C PTS: 1 TOP: Enzyme Inhibition 69. Irreversible
inhibitors of enzymatic reactions
a. bind to the enzyme only at low temperatures.
b. affect only serine side chains.
c. react with the enzyme to produce a protein that is not enzymatically active and from which
the original enzyme cannot be regenerated.
d. are bound to the enzyme by the lock-and-key mechanism.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Enzyme Inhibition
70. A noncompetitive inhibitor
a. binds to the enzyme at a site other than the active site
b. is structurally related to the substrate
c. does not affect the value of Vmax
d. decreases the value of KM
ANS: A PTS: 1 TOP: Enzyme Inhibition 71. What effect is seen
on a Lineweaver-Burk graph when a competitive inhibitor is added?
a. The y-intercept is changed, but not change the slope of the line.
b. The slope of the line is changed, but not the y-intercept.
c. Both the y-intercept and the slope of the line are changed.
d. Neither the y-intercept not the slope of the line is changed.
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Enzyme Inhibition
72. What effect is seen on a Lineweaver-Burk graph when a mixed-type inhibitor is
added?
a. The y-intercept is changed, but not change the slope of the line.
b. The slope of the line is changed, but not the y-intercept.
c. Both the y-intercept and the slope of the line are changed.
d. Neither the y-intercept not the slope of the line is changed.
ANS: C PTS: 1 OBJ: New in 6e TOP: Enzyme Inhibition 73.
Generally speaking, a competitive inhibitor and the substrate cannot both bind to the enzyme at the
same time.
a. True
b. False
ANS: A PTS: 1 TOP: Enzyme Inhibition 74. What effect is seen
on a Lineweaver-Burk graph when a non-competitive inhibitor is added?
a. The y-intercept is changed, but not change the slope of the line.
b. The slope of the line is changed, but not the y-intercept.
c. Both the y-intercept and the slope of the line are changed.
d. Neither the y-intercept not the slope of the line is changed.
ANS: A PTS: 1 OBJ: New in 6e TOP: Enzyme Inhibition 75.
Non-competitive inhibitors have this effect:
a. Modifying the KM value.
b. Changing the value for Vmax.
c. Interfering with substrate binding.
d. This type of inhibitor both changes the Vmax and interferes with substrate binding.
e. All of these are correct.
ANS: B PTS: 1 TOP: Enzyme Inhibition 76. If an inhibitor
changes the slope of the Lineweaver-Burk graph, but not the y-intercept, it is this type of inhibition:
a. Competitive.
 b. Non-competitive.
c. Mixed Inhibition (uncompetitive inhibition).
d. You cannot tell from the data given.
e. More than one answer is correct.
ANS: A PTS: 1 TOP: Enzyme Inhibition 77. If an inhibitor
changes the slope of the Lineweaver-Burk graph, but not the x-intercept, it is this type of inhibition:
a. Competitive.
b. Non-competitive.
c. Mixed Inhibition (uncompetitive inhibition).
d. You cannot tell from the data given.
e. More than one answer is correct.
ANS: B PTS: 1 TOP: Enzyme Inhibition 78. Which of the
following diseases has not been successfully treated using the principles of enzyme inhibition?
a. AIDS.
b. Lactose intolerance
c. Virus infection
d. Neither AIDS nor virus infection.
e. All of these have been successfully treated using enzyme inhibitors.
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Enzyme Inhibition
Chapter 7—The Behavior of Proteins: Enzymes, Mechanisms, and Control MULTIPLE
CHOICE 1. Which of the following best describes negative cooperativity?
a. Binding of one substrate molecule prevents the enzyme from working at all.
b. Binding of one substrate molecule inhibits the binding of a second substrate.
c. Binding of one substrate molecule enhances the binding of a second substrate.
d. Binding of one substrate molecule inhibits the binding of other effectors.
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Behavior of Allosteric
Enzymes 2. The saturation curve for aspartyl transcarbamylase has a similar shape to the
curve for:
a. Myoglobin
b. Hemoglobin
c. Chymotrypsin
d. Both hemoglobin and chymotrypsin.
e. All of these.
ANS: B PTS: 1 TOP: Behavior of Allosteric Enzymes 3. CTP is a known
inhibitor of ATCase, the enzyme that catalyzes the first reaction in the pathway for the synthesis of this
compound. This is an example of
a. irreversible inhibition
b. feedback inhibition
c. zymogenic inhibition
d. negative cooperativity
ANS: B PTS: 1 OBJ: New in 6e TOP: Behavior of Allosteric Enzymes 4.
Homotrophic effects for allosteric enzymes involve
a. the same molecule binding to different sites in the enzyme.
b. different molecules binding to the same site in an enzyme.
c. different molecules binding to different sites in the same enzyme.
d. All of these are homotrophic effects.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Behavior of Allosteric
Enzymes 5. Enzyme kinetics falls into two general categories, simple saturation and
cooperative kinetics.
a. True
b. False
 ANS: A PTS: 1 TOP: Behavior of Allosteric Enzymes NARRBEGIN: Exhibit 7A
Exhibit 7A
M → N → O → P → Q → R
1 2 3 4 5
NARREND 6. Refer to Exhibit 7A. The final product, R, will most likely inhibit which
reaction?
a. 1
b. 2
c. 3
d. 4
e. 5
ANS: A PTS: 1 TOP: Behavior of Allosteric Enzymes 7. Refer to Exhibit
7A. Which two enzymes would be the most likely ones to regulate if this pathway is dedicated to the
formation of only one product?
a. 1 and 2
b. 1 and 3
c. 1 and 5
d. 2 and 4
e. 4 and 5
ANS: A PTS: 1 TOP: Behavior of Allosteric Enzymes 8. Refer to Exhibit
7A. Which two enzymes would be the most likely ones to regulate if this pathway is freely reversible
and can go both ways?
a. 1 and 2
b. 1 and 3
c. 1 and 5
d. 2 and 4
e. 4 and 5
ANS: C PTS: 1 TOP: Behavior of Allosteric Enzymes 9. Which of the
following is a mechanism of regulating enzyme activity?
a. Feedback inhibition by product.
b. Addition or removal of phosphate groups from of the enzyme.
c. Presence of activators.
d. Activation of zymogens.
e. All of these regulate enzyme activity.
ANS: E PTS: 1 OBJ: Modified from 5e TOP: Behavior of Allosteric
Enzymes 10. Which of the following is true?
a. Allosteric enzymes are rarely important in the regulation of metabolic pathways.
b. Michaelis-Menten kinetics describe the reactions of allosteric enzymes
c. Allosteric enzymes have a hyperbolic plot of reaction rate vs. substrate concentration
d. none of these is true
ANS: D PTS: 1 OBJ: New in 7e TOP: Behavior of Allosteric Enzymes 11.
Which of the following is not required in order for an enzyme to display cooperative kinetics?
a. Multiple subunits.
b. A value for the Michaelis constant, KM.
c. Allosteric sites which affect the binding of substrate to the active site.
d. Ability to display a Vmax.
e. All of these are characteristic of cooperative enzymes.
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Behavior of Allosteric
Enzymes 12. In a comparison of allosteric and non-allosteric enzymes
a. it is always possible to define a KM
 b. it is always possible to define a Vmax
c. competitive inhibition is always a possibility
d. much of the terminology is completely unchanged
ANS: B PTS: 1 TOP: Behavior of Allosteric Enzymes 13. Is the Michaelis-
Menten equation useful when studying allosteric enzymes?
a. Yes
b. No
c. Only if the enzyme displays positive cooperativity.
d. Only if the enzyme displays negative cooperativity.
ANS: B PTS: 1 OBJ: Modified from 5e TOP: Behavior of Allosteric
Enzymes 14. Where do allosteric inhibitors bind on an enzyme?
a. They always bind at a site different from the active site.
b. They always bind at the active site.
c. They can bind at either active site or another site.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Behavior of Allosteric
Enzymes 15. The term K0.5 is analogous to the KM
a. True
b. False
ANS: A PTS: 1 TOP: Behavior of Allosteric Enzymes 16. How do each of
these compounds affect the function of ATCase?
a. ATP inhibits and CTP activates
b. ATP activates and CTP inhibits
c. Both ATP and CTP inhibit
d. Both ATP and CTP activate
ANS: B PTS: 1 OBJ: New in 6e TOP: Behavior of Allosteric Enzymes 17.
How do each of these compounds affect the function of ATCase?
a. ATP is a K effector and CTP is a V effector.
b. ATP V effector and CTP K effector.
c. Both ATP and CTP are K effectors.
d. Both ATP and CTP are V effectors.
ANS: C PTS: 1 OBJ: New in 6e TOP: Behavior of Allosteric Enzymes 18.
In reactions catalyzed by allosteric enzymes
a. substrate, activators, and inhibitors all compete for the same binding site on the enzyme.
b. there is no distinction between catalytic and regulatory subunits.
c. the presence of an activator makes the plot of reaction rate against substrate concentration
less cooperative.
d. the presence of an inhibitor makes the plot of reaction rate against substrate concentration
less cooperative.
ANS: C PTS: 1 TOP: Behavior of Allosteric Enzymes 19. A velocity curve (V
vs. [S]) for a typical allosteric enzyme will be
a. a rectangular hyperbola.
b. a sigmoid curve.
c. a straight line.
d. a parabola.
ANS: B PTS: 1 TOP: Behavior of Allosteric Enzymes 20. ATP is a negative
allosteric effector for glycogen phosporylase. This is an example of
a. feedback inhibition.
b. positive cooperativity.
c. negative cooperativity.
d. competitive inhibition.
ANS: A PTS: 1 TOP: Behavior of Allosteric Enzymes 21. Many metabolic
pathways involve multistep reactions. Consider the following pathway.
E1 E2 E3 E4
A → B → C → D → F (final product)
Which of the following would be an example of feedback inhibition?
a. the product of the final reaction, F, interacting with E1.
b. F interacting with an allosteric site in E4.
c. B interacting with an allosteric site in E1.
d. all of the intermediates or products in the reaction interacting with the active site in E1.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Behavior of Allosteric
Enzymes 22. Allosteric effectors
a. typically bind to the enzyme's active site.
b. typically bind at a site unique from the active site.
c. bind to the substrate rather than the enzyme.
d. only bind to the enzyme-substrate complex.
ANS: B PTS: 1 TOP: Behavior of Allosteric Enzymes 23. Allosteric enzymes
must exhibit which of the following?
a. feedback inhibition
b. a phosphorylation site
c. general acid-base catalysis
d. a quaternary structure
ANS: D PTS: 1 TOP: Behavior of Allosteric Enzymes 24. What happens when
a K-acting inhibitor is added to an allosteric enzyme system?
a. The apparent KM for the substrate increases.
b. The apparent KM for the substrate decreases.
c. The apparent Vmax for the substrate increases.
d. The apparent Vmax for the substrate decreases.
ANS: A PTS: 1 TOP: Behavior of Allosteric Enzymes 25. The behavior of
allosteric enzymes
a. does not play any role in feedback inhibition in metabolic pathways
b. is strongly dependent on the presence of metal ions
c. is related to their ability to hydrolyze themselves
d. depends on changes in their quaternary structure on binding of substrates or inhibitors
ANS: D PTS: 1 TOP: Behavior of Allosteric Enzymes 26. The concerted model
for allosteric behavior was proposed by:
a. Koshland
b. Pauling
c. Pasteur
d. Monod, Wyman and Changeux
e. All of these
ANS: D PTS: 1 OBJ: Modified from 5e TOP: Allosteric Models
27. The sequential model for allosteric enzymes was proposed by:
a. Koshland
b. Pauling
c. Pasteur
d. Monod, Wyman and Changeux
e. All of these
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Allosteric Models
28. Which of the following does not apply to the concerted model for subunit behavior:
a. Each subunit can exist in a relaxed (R) and taut (T) conformation.
 b. All subunits will be in either the R or the T conformation at the same time.
c. Some subunits can be in the R state while others are in the T state.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Allosteric Models
29. In the concerted model for allosteric enzymes
a. the relative affinities of substrate for the T and R conformations plays an important role in
the cooperativity of the reaction.
b. the equilibrium between the T and R conformations plays a minor role.
c. the enzymatic activity of the T conformation is considerably higher than that of the R form.
d. it is possible to describe the reactions of all allosteric enzymes accurately.
ANS: A PTS: 1 TOP: Allosteric Models 30. In the concerted
model, which state binds the substrate more tightly?
a. the relaxed (R) state
b. the taut (T) state
c. Both states bind equally well.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Allosteric Models
31. The sequential model for allosteric behavior
a. cannot account for reactions that display negative cooperativity.
b. postulates binding of substrates and inhibitors by the induced-fit model.
c. requires that the conformation of all subunits change simultaneously.
d. is mathematically simpler than the concerted model.
ANS: B PTS: 1 TOP: Allosteric Models 32. In the concerted
model the binding of the first substrate molecule will achieve all except
a. facilitation of the binding of other substrate molecules.
b. facilitation of the conversion of other subunits to the active state.
c. facilitation of the binding of inhibitors to the enzyme.
d. All of these are facilitated by the binding of the first substrate molecule.
e. None of these answers is correct.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Allosteric Models
33. In the concerted model the most active enzyme form will be when
a. all subunits are in the R state.
b. all subunits are in the T state.
c. there is a 50:50 mix of R & T states.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Allosteric Models
34. According to the concerted model of allosteric behavior, an allosteric activator
a. favors the taut (tight) form of the enzyme.
b. favors the relaxed form of the enzyme.
c. can only bind to the enzyme if the substrate is already bound.
d. can only bind to the enzyme if the substrate has not already bound.
ANS: B PTS: 1 TOP: Allosteric Models 35. The concerted and
sequential models for the behavior of allosteric enzymes differ in
a. the conformational change in the enzyme in one model and not in the other.
b. the number of predicted binding sites on the enzyme.
c. the manner in which changes in quaternary structure take place.
d. the response of the enzyme to changes in temperature.
ANS: C PTS: 1 TOP: Allosteric Models 36. Which of the
following is not a difference between the concerted model and the sequential model of allosteric
enzymes?
a. The sequential model allows for different subunits to be in different conformations while
the concerted model does not
b. Negative cooperativity can be explained by the sequential model but not by the concerted
model
 c. Positive cooperativity can be explained by the sequential model but not by the concerted
model
d. The sequential model is explained better by considering the induced-fit model of substrate
binding, whereas the concerted model focuses on perturbing the equilibrium between the T
and R forms.
ANS: C PTS: 1 OBJ: New in 7e TOP: Allosteric Models 37. The
main distinguishing feature of the concerted model for the behavior of allosteric enzymes is that
a. the conformation of all subunits changes simultaneously.
b. it applies only to dimeric enzymes.
c. it involves three possible conformations for all subunits.
d. the T and R conformations exist in roughly equal amounts.
ANS: A PTS: 1 TOP: Allosteric Models 38. Kinase reactions
describe enzymes which
a. add phosphate groups to another molecule.
b. oxidize alcohols to aldehydes.
c. use NAD+/NADH in their reactions.
d. transfer groups from one part of a molecule to another.
e. add or remove double bonds in molecules.
ANS: A PTS: 1 OBJ: New in 6e TOP: Enzyme Regulation by Phosphoryla-
tion 39. Kinases usually transfer phosphates from
a. ATP.
b. inorganic phosphate.
c. NADP+/NADPH.
d. amino acids.
ANS: A PTS: 1 OBJ: New in 6e TOP: Enzyme Regulation by Phosphoryla-
tion 40. Generally speaking, enzymes involved in pathways which generate ATP will
be activated by addition of phosphate groups to the enzyme.
a. True
b. False
ANS: B PTS: 1 TOP: Enzyme Regulation by Phosphorylation 41. Which of the
following is true?
a. Phosphorylation always increases enzyme activity
b. Kinases often use AMP as a co-substrate in their phosphorylation reactions
c. Some enzymes are activated by phosphorylation while others are inhibited
d. ADP is the most common substrate for a kinase reaction
ANS: C PTS: 1 OBJ: New in 7e TOP: Enzyme Regulation by Phosphoryla-
tion 42. Phosphorylation and allosteric control of enzymes.
a. are not involved in reactions of carbohydrates.
b. play an insignificant role in generating energy.
c. are important processes in prokaryotes, but not in eukaryotes.
d. can be combined to afford a high degree of control over enzymatic reactions.
ANS: D PTS: 1 TOP: Enzyme Regulation by Phosphorylation 43. Phosphory-
lation of enzymes
a. has no effect on their catalytic activity.
b. does not require ATP.
c. usually takes place on serine, threonine, and tyrosine residues.
d. is not easily characterized.
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Enzyme Regulation by
Phosphorylation 44. Zymogens are
a. inactive precursors of enzymes which can be activated by the irreversible cleavage of
covalent bonds.
 b. inactive forms of enzymes which require phosphorylation by a kinase to become active.
c. allosteric enzymes that are always in the R state.
d. allosteric enzymes that are always in the T state.
ANS: A PTS: 1 OBJ: New in 6e TOP: Zymogens 45. In zymogen
activation
a. only digestive enzymes are involved.
b. a conformational change takes place with no alteration of primary structure.
c. an inactive protein is converted to an active one by bond cleavage.
d. there is aggregation of several enzyme molecules when the substrate binds.
ANS: C PTS: 1 TOP: Zymogens 46. Which of the following is true?
a. Caspases are a class of proteases
b. Caspases are involved in apoptosis
c. Caspases are initially produced as inactive procaspases
d. all of these
ANS: A PTS: 1 OBJ: New in 7e TOP: Zymogens 47. Which of the
following types of amino acids active is least likely to be involved in enzyme catalysis?
a. Those with hydrophilic, neutral side-chains.
b. Those with negatively charged side-chains.
c. Those with positively charge side-chains.
d. Those with hydrocarbon side-chains.
ANS: D PTS: 1 OBJ: New in 6e TOP: Nature of the Active Site 48.
Inhibitors which bind covalently to specific amino acids are useful in determining which
amino acids are in the active site of an enzyme.
a. True
b. False
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Nature of the Active Site
49. Which of the following enzymes is not a serine protease?
a. trypsin
b. chymotrypsin
c. thrombin
d. aspartyl transcarbamylase (ATCase)
ANS: D PTS: 1 OBJ: New in 6e TOP: Nature of the Active Site 50.
The initial bond formation in the covalent intermediate in the reaction catalyzed by chy-
motrypsin is between
a. serine and the carbonyl carbon in the peptide backbone
b. serine and the nitrogen in the peptide backbone
c. histidine and the carbonyl carbon in the peptide backbone
d. histidine and the nitrogen in the peptide backbone
ANS: A PTS: 1 TOP: Nature of the Active Site 51. An important step in
elucidating the behavior of an enzyme is
a. obtaining a crystalline sample of the enzyme.
b. insuring that metal ions are always excluded from the enzyme sample.
c. determining the active site residues.
d. none of these
ANS: C PTS: 1 OBJ: Modified in 7e TOP: Nature of the Active Site
52. The amino acids in the active site can be involved in all of these processes, except:
a. Binding of the substrate.
b. Becoming part of the product of the reaction.
c. The actual chemical mechanism for the reaction.
d. Binding of some necessary cofactor for the reaction.
e. All of these can be functions of the amino acids in the active site
 ANS: B PTS: 1 TOP: Nature of the Active Site 53. The critical serine
residue in the active site of chymotrypsin functions as
a. a nucleophile.
b. an electrophile.
c. a base.
d. a methyl donor.
ANS: A PTS: 1 OBJ: New in 6e TOP: Nature of the Active Site 54.
The active site of chymotrypsin contains all of the following, except:
a. Histidine residue.
b. A magnesium ion.
c. Hydrophobic pocket to bind the substrate.
d. Serine residue.
e. All of these are in the active site of chymotrypsin.
ANS: B PTS: 1 TOP: Nature of the Active Site 55. The pH profile of an
enzyme can help identify specific amino acids in the active site because:
a. all enzymes have a pH optimum
b. only the active site amino acids can detect changes in pH
c. acidic and basic amino acids are often involved in the active site and pH changes can
change their ability to catalyze a reaction
d. the pH optimum is always the pI of the most critical amino acid in the active site
ANS: C PTS: 1 OBJ: New in 7e TOP: Nature of the Active Site 56.
Which groups of amino acids are likely to be found in the active site of an enzyme?
a. leucine, lysine, alanine.
b. cysteine, isoleucine, phenylalanine.
c. tyrosine, threonine, leucine.
d. serine, histidine, aspartate.
ANS: D PTS: 1 TOP: Nature of the Active Site 57. Labeling the amino
acid residues in the active site of an enzyme requires
a. a reagent structurally similar to the substrate.
b. a highly polar reagent.
c. a reagent that contains an aromatic group.
d. a reagent that contains a halogen atom.
ANS: A PTS: 1 TOP: Nature of the Active Site 58. Which of the
following is unlikely to occur in binding of a substrate to an enzyme?
a. stereospecific interactions.
b. hydrogen bonding.
c. adsorption to surfaces of metallic catalysts.
d. interactions with metal-ions.
ANS: C PTS: 1 TOP: Nature of the Active Site 59. Which of the
following amino acid side chains would best serve as a general acid, assuming the protein functions at
a pH of 7?
a. alanine
b. aspartic acid
c. lysine
d. asparagine
ANS: C PTS: 1 TOP: Types of Chemical Reactions 60. Metal ions play an
important role in reaction mechanisms because
a. they block the active site of enzymes so that inhibitors cannot bind.
b. they can act as Lewis acids.
c. water is excluded from the active site when metal ions are bound.
d. they prevent protein aggregation.
ANS: B PTS: 1 TOP: Types of Chemical Reactions 61. The serine in the
active site of chymotrypsin functions as
a. a Lewis acid.
b. a metal ion.
c. an electrophile.
d. a nucleophile.
ANS: D PTS: 1 TOP: Types of Chemical Reactions 62. Important mecha-
nisms of enzymatic catalysis include
a. nucleophilic reactions
b. general acid-base catalysis
c. Lewis acid-base catalysis
d. all of these
ANS: D PTS: 1 OBJ: Modified in 7e TOP: Types of Chemical Reactions
63. Enzymes that catalyze similar functions will invariably have
a. similar overall structures.
b. serine in their active sites.
c. histidine in their active sites.
d. active sites that can catalyze the reactions in question.
ANS: D PTS: 1 TOP: Types of Chemical Reactions 64. A transition-state
analog is likely to bind to an enzyme
a. more tightly than the substrate.
b. less tightly than the substrate.
c. about as tightly as the substrate.
d. at a site other than the catalytic site.
ANS: A PTS: 1 OBJ: New in 6e TOP: Active Site and Transition States
65. Abzymes
a. invariably bind to pyridoxal phosphate.
b. are antibodies with catalytic activity.
c. differ markedly from transition states in enzymatic reactions.
d. have proline as part of their structure.
ANS: B PTS: 1 TOP: Active Site and Transition States 66. How are
cofactors bound to their enzymes?
a. always covalently
b. always non-covalently
c. either covalently or non-covalently
ANS: C PTS: 1 OBJ: Modified from 5e TOP: Coenzymes 67.
Which of the following is not true about B vitamins?
a. They are usually fully active in the form we eat them
b. They are usually water soluble
c. Niacin and riboflavin are examples
d. They are important in many metabolic reactions
ANS: A PTS: 1 OBJ: New in 7e TOP: Coenzymes 68. Cofactors
are
a. non-protein in chemical nature.
b. always small proteins.
c. modified amino acids.
d. never required for enzymatic activity.
ANS: A PTS: 1 OBJ: Modified from 5e TOP: Coenzymes 69.
Nicotinamide adenine dinucleotide is
a. an enzyme inhibitor used in smoking cessation programs.
b. an inhibitor of ATP production.
 c. a coenzyme in reactions that transfer acyl groups.
d. a coenzyme in oxidation-reduction reactions.
ANS: D PTS: 1 TOP: Coenzymes 70. Which of the following statements
about coenzymes is true?
a. They are commonly derived from vitamins.
b. They bind to the active site region on specific types of enzymes.
c. They can be metal ions, such as Zn(II).
d. NAD+, FAD and biotin are all examples of coenzymes.
e. All of these statements are true.
ANS: E PTS: 1 OBJ: Modified from 5e TOP: Coenzymes 71. The
vitamin biotin is involved in this type of reaction:
a. Carboxylation reactions
b. Decarboxylation reactions
c. Redox reactions
d. Acyl transfer reactions
e. Transamination reactions
ANS: A PTS: 1 TOP: Coenzymes 72. Redox reactions often use this
cofactor:
a. Riboflavin
b. Lipoic acid
c. Pyridoxal
d. Thiamine
e. Biotin
ANS: A PTS: 1 TOP: Coenzymes 73. Which of the following can function
as coenzymes?
a. lead ion, biotin, and lipoic acid.
b. copper ion, p-hydroxymercuribenzoate, diisopropylphophofluoridate.
c. zinc ion, pyridoxal phosphate, and nicotinamide adenine nucleotides.
d. lead ion, p-hydroxymercuribenzoate, diisopropylphophofluoridate.
ANS: C PTS: 1 TOP: Coenzymes 74. The vitamin pantothenic acid is
involved in this type of reaction:
a. Carboxylation reactions
b. Decarboxylation reactions
c. Redox reactions
d. Acyl transfer reactions
e. Transamination reactions
ANS: A PTS: 1 TOP: Coenzymes 75. Pyridoxal phosphate is required for
transfer of
a. one-carbon groups
b. amino groups
c. acyl groups
d. aldehyde groups
ANS: B PTS: 1 TOP: Coenzymes 76. B vitamins are often stored in the
body.
a. True
b. False
ANS: B PTS: 1 TOP: Coenzymes 77. Acyl transfer reactions often use this
cofactor:
a. Riboflavin
b. Lipoic acid
c. Pyridoxal