Lehninger Biochemistry 4e Ch 01

1.. A dynamic steady state results when

D. a carboxyl group.
6. Which of the following is true about the two molecules shown

A. a molecule stops being degraded.

below?

B. an organism is at equilibrium with its surroundings.

C. there is no net energy transfer.
D. the rate of intake or synthesis of a molecule equals the
rate of its disappearance.
2. An open system is one
A. that exchanges neither matter nor energy with its
surroundings.
B. that exchanges energy but not matter with its

A. They have the same configuration.

B. They are cis-trans isomers.

surroundings.
C. They are enantiomers of each other.
C. that exchanges both matter and energy with its
surroundings.

D. They are diastereomers of each other.

D. that exchanges matter but not energy with its

surroundings.
3. Which of the following is true about the energy from sunlight?
A. All organisms obtain their energy directly from the radiant
energy of sunlight.
B. Photosynthetic cells use light energy to drive electrons
from one molecule to another.
C. Energy from sunlight is given off in nuclear fission
reactions in the sun.
D. Photosynthetic cells absorb light energy and use it to break
down compounds such as starch and sucrose.

7. Which of the following is true about the two molecules shown

above?
A. They are geometric isomers.
B. The carbon double bonds in each are chiral centers.

4. Which of the following is true about carbon bonding?

C. Fumaric acid is a cis-isomer of maleic acid.
A. Carbon-carbon double bonds have freedom of rotation.
D. They can be interconverted without breaking any covalent
B. Carbon atoms can form covalent bonds with up to four
other atoms.
C. Carbon can form double bonds with hydrogen.
D. Carbon-carbon single bonds cannot rotate.

bonds.
8. The difference between phototrophs and chemotrophs is
A. whether they are aeorbic or anaerobic.
B. their energy source.

5. The amino acid alanine, shown below, contains all of the

following functional groups except

C. their source of carbon.

D. whether they are prokaryotic or eukaryotic.
9. Prokaryotic and eukaryotic cells possess which of the following?
A. a cytoskeleton
B. a nuclear envelope

A. an amino group.
B. a methyl group. Incorrect.

C. mitochondria
D. a plasma membrane
10. Exergonic and endergonic reactions differ in that

C. an ester group.
A. exergonic reactions have a positive free energy change (

G is positive) and endergonic reactions have a negative free energy

change ( G is negative).
B. exergonic reactions require an input of energy and
endergonic reactions release free energy.
C. exergonic reactions produce products with less free energy
than the reactants; endergonic reactions produce products with
more free energy than the reactants.
D. exergonic reactions consume more free energy than is

A. if it has no stereoisomers
B. if the molecule that it belongs to can be superimposed on
its mirror image after rotation
C. if it is symmetric
D. if it has four different substituent groups
16. Which of the following is true about stereoisomers?
A. They have different configurations.

released and endergonic reactions release more free energy than is

consumed.
11. The three-dimensional structure (native conformation) of

B. They are indistinguishable by enzymes.

C. The have different chemical bonds.

proteins is determined primarily by

D. They exist in equal amounts in living organisms.
A. noncovalent interactions.

17. Genetic material in the form of DNA is not present in

B. the other proteins with which it forms a complex.

A. chloroplasts.

C. its amino acid sequence.

B. the nucleus.

D. molecular chaparones.

C. ribosomes.

12. Which of the following is true of metabolism?

D. mitochondria.
A. Degradative reactions require an input of energy.
B. Synthetic pathways are anabolic.
C. Catabolism and anabolism are linked by O2.
D. Catabolic reactions require the breakdown of ATP, and
anabolic reactions generate ATP.
13. Which of the following is true about how enzymes work in the
cell?

18. Paralogs and orthologs differ in that

A. Paralogs have the same amino acid sequence and
orthologs have different amino acid sequences.
B. Paralogs exist in the same species and orthologs exist in
different species.
C. Paralogs have the same function and orthologs have
different functions.

A. Enzymes are consumed in the process of converting one

molecule to another.
B. Enzymes are needed to carry out only endergonic
reactions.
C. Enzymes are needed in the cell to increase the rate of a
chemical reaction.
D. Enzymes eliminate the activation barrier.

D. Paralogs have the same three-dimensional structure and

orthologs have different three-dimensional structures.
19. Supramolecular complexes of proteins, nucleic acids, and
polysaccharides are not held together by
A. ionic interactions.
B. hydrogen bonds.
C. hydrophobic interactions.

14. How can thermodynamically unfavorable reactions, such as the

synthesis of DNA and protein polymers, occur in cells?

D. covalent bonds.
Lehninger Biochemistry 4e Ch 02

A. Cells couple thermodynamically unfavorable reactions to

1. Which of the gases in the table below is most polar?

reactions that result in a positive change in enthalpy.

B. Cells couple thermodynamically unfavorable reactions to
the hydrolysis of ATP.
C. Cells couple thermodynamically unfavorable reactions to
reactions that have a positive free energy.
A. carbon dioxide
D. Cells couple thermodynamically unfavorable reactions to
reactions that result in a decrease in entropy.
15. Under what conditions is a carbon atom a chiral center?

B. hydrogen sulfide
C. oxygen

D. nitrogen

D. Cells can neither shrink nor swell because water cannot

2. In ice, each water molecule forms hydrogen bonds with four

penetrate the plasma membrane.

other water molecules, as compared to liquid water in which each

8. Which of the following is true about acids and bases?

water molecule forms hydrogen bonds with 3.4 other water

A. When bases ionize, they donate protons. (see p. 63)

molecules. A consequence of this is that

B. Strong acids and bases are completely ionized in dilute

A. ice is more dense than water.

aqueous solutions.
B. water has a relatively low boiling point.
C. The dissociation constant of a strong acid is lower than that
C. water has a relatively high melting point.

for a weak acid.

D. water turning into ice is a spontaneous reaction because

D. The pKa of a strong acid will be higher than that for a weak

more hydrogen bonds are involved in ice.

acid.

3. Which of the following is true about hydrogen bonds?

9. Cells need to be buffered because

A. Hydrogen bonds are longer and stronger than covalent

bonds.
B. The geometry of a water molecule results in the equal

A. they need to be able to increase or decrease their cytosolic

pH to adapt to various environmental conditions.
B. their proteins work best at low pH.

sharing of electrons between the hydrogen and oxygen. (see p. 48)

C. they need to maintain a specific cytosolic pH to keep
C. Hydrogen bonds must involve at least one water molecule.
D. Polar molecules are soluble in water because they can form

biomolecules from being ionized.

D. they need to maintain a specific cytosolic pH to keep

hydrogen bonds with water molecules.

biomolecules at their optimal ionic state.

4. Micelles are characteristic of what kinds of molecules?

10. Which of the following is true about condensation reactions?

A. nonpolar molecules
B. charged molecules

A. Condensation reactions are invariably exergonic.

B. Condensation reactions involve the depolymerizion of
macromolecules.

C. amphipathic molecules
C. Condensation reactions involve the loss of the elements of
D. polar molecules

water.

5. What is the concentration of H+ in a pH 0 solution of acid?

D. A typical condensation reaction is the formation of ADP
A. 0 M
B. 1 M

from ATP and inorganic phosphate.

11. Hydrophobic interactions account for

C. 1 X 10-7 M

A. why biomolecules are amphipathic.

D. 1 X 10-14 M

B. why the nonpolar regions of molecules cluster together in

6. What is the concentration of H+ in a solution of 0.01M NaOH?

A. 0.01M
B. 2 M

water.
C. the tendency of lipids to disperse in water.
D. why the polar regions of molecules are associated with
water.

C. 10-12 M
D. 10-2 M
7. Osmosis is water movement across a semipermeable membrane.

12. Based on the Henderson-Hasselbalch equation (shown below),

calculate the pH when the ratio of acetic acid to acetate is 10 to 1
(the pKa of acetic acid is 4.76).

Which of the following is true about water movement across cell

membranes?
A. In a hypotonic solution, cells will swell.
B. In an isotonic solution, cells will shrink.
A. 1.00
C. In a hypertonic solution, cells will stay the same.
B. 3.76

C. 4.76

B. NaCl does not spontaneously dissolve in water because the

Na+ and Cl- ions are in the form of a stable crystalline lattice.

D. 5.76
13. Which of the following pairs of groups cannot form a hydrogen
bond with each other (the proposed hydrogen bond is indicated by

C. Crystalline salts dissolve in water because it results in an

increase in entropy.

the blue rectangle)?

D. Crystalline salts dissolve in water because water adds to
A.

the electrostatic attractions of Na+ and Cl- ions.

15. Based on the Henderson-Hasselbalch equation (shown below),
calculate the pH when the ratio of acetic acid is half dissociated to
acetate (the pKa of acetic acid is 4.76).

A. 1.00
B.

B. 3.76
C. 4.76
D. 5.76
16. A buffer system consists of
A. a weak acid and its conjugate base.
B. a weak acid and a proton donor.
C. a weak acid and a proton.

C.
D. a weak base and a proton acceptor.
17. Which of the following is true about the titration curves of
solutions of weak acids?
A. The pH for optimal buffering power of a weak acid is 7.00.
B. You can calculate the pKa of an acid, given the pH and the
molar ratio of the acid and its conjugate base.
C. The pKa of a weak acid is the pH at which the acid is
completely dissociated.
D. At a pH below the pKa of a weak acid, its conjugate base
D.

will predominate.
Lehninger Biochemistry 4e Ch 03
1. At the center of all 20 standard amino acids is what is termed
the -carbon that is covalently bonded with four other chemical
groups. Which of these four chemical groups is not a normal
component of all amino acids?
A. an amino group
B. a carboxyl group
C. a side chain (R group)

14. Which of the following is true about how crystalline salts, such
as NaCl, behave in water?
A. Water can form hydrogen bonds with NaCl.

D. a methyl group
2. L-alanine and D-alanine
A. are present in virtually all proteins.

B. are superimposable isomers of each other.

A. glycine

C. are enantiomers.

B. threonine

D. lack an R group.

C. aspartate

3. Cysteine residues play an important role in the structure of many

proteins by

D. arginine
7. The isoelectric point, or pI, of an amino acid or a protein is

A. providing covalent links between parts of a protein

molecule or between two different protein chains.

A. the pH at which the amino acid or protein has no net

charge.

B. forming disulfide bonds with another amino acid.

B. zero at pH 7.0.
C. linking two protein chains through hydrophobic
interactions.

C. the pH at which the amino acid or protein is neither

hydrophobic nor hydrophilic.

D. reducing two cysteine residues.

4. A polypeptide is cleaved into peptides by treatment with trypsin
and cyanogen bromide, and the peptides are purified and
sequenced. The sequences of the peptides (from N to C-terminus)

D. the measure of the hydropathy of an amino acid or protein.

8. Peptide bonds, which covalently link two amino acids, result from
A. the oxidation of amino acids.

are shown below. (Note: Trypsin cleaves after K and R residues;

cyanogen bromide cleaves after M.)

B. the condensation of amino acids.

C. the hydrolysis of amino acids.
D. hydrogen bonds between amino acids.
9. Which group or groups on a protein contribute most to its overall
acid-base properties?
A. The -amino groups of all nonterminal amino acids.

Based on sequences of the overlapping peptides generated by

treatment with trypsin and cyanogen bromide (shown above),
which of the peptides could represent the N-terminus of the
polypeptide?
A. T-3
B. C-1
C. C-2

B. The N-terminal -amino group on the protein.

C. The R groups on the protein.
D. The C-terminal -carboxyl group on the protein.
10. Human hemoglobin has four polypeptide subunits: two identical
16,000 molecular weight -chains and two identical 16,000
molecular weight -chains, whereas the RNA polymerase of
influenza virus has three unique polypeptide subunits: PA, PB1 and
PB2. Which of the following statements is true?

D. T-4
5. Because proteins can absorb light maximally at 280 nm, they
can be identified and quantified in solution by using a
spectrophotometer. Which of the following is true about the
absorption of light by proteins?
A. Proteins absorb infrared light.
B. All amino acids absorb light equally.
C. The greater the concentration of protein in a solution, the
more 280 nm transmitted light will be detected by a
spectrophotometer.
D. Absorbance of 280 nm light by proteins increases with the
concentration of the protein.
6. Which of the following amino acids has a net negative charge at

A. Influenza virus RNA polymerase consists of protomers.

B. Human hemoglobin and influenza virus RNA polymerase
are oligomeric proteins.
C. Human hemoglobin and influenza virus RNA polyperase are
multisubunit proteins.
D. Human hemoglobin consists of oligopeptide subunits.
11. The level of protein structure that describes all aspects of the
three-dimensional folding of a polypeptide is referred to as the
A. quaternary structure.
B. secondary structure.
C. primary structure.

pH 7.0?
D. tertiary structure.

12. A protein retained on an affinity chromatography column is

B. Peptides are synthesized in an N-terminal to C-terminal

usually eluted off the column by

direction.
A. gradually increasing the salt concentration of the elution
C. Peptides must be purified (isolated) after each addition

buffer.
cycle.
B. adding the protein's free ligand.

D. Peptides of any length can be synthesized.

C. changing the pH of the elution buffer.

18. Which of the following is true about the Edman degradation

system of sequencing polypeptides?

D. allowing the retained protein to naturally come off the

column after the non-specifically bound proteins have first passed
through the resin.

A. The Edman degradation system will work on any size

polypeptide.

13. Which of the following is not true about SDS polyacrylamide

gel electrophoresis of proteins?

B. In the Edman degradation system the amino-terminal

residue is labeled and the polypeptide is hydrolyzed to its

A. Polyacrylamide acts as a molecular sieve.

B. It separates charged proteins by using an electric field.

constituent amino acids.

C. In the Edman degradation system the amino-terminal
residue is labeled, cleaved and identified in each successive cycle.

C. Larger proteins move faster in the gel than smaller

proteins.

D. The Edman degradation system is carried out on a machine

called an edmanator.

D. It separates proteins that differ in molecular weight.

14. Sodium dodecyl sulfate (SDS) is used in the electrophoresis of
proteins to
A. separate the subunits of a multisubunit protein.
B. bind proteins and confer a large net positve charge.
C. change the charge-to-mass ratio of proteins.
D. help proteins adopt a native conformation.
15. Two proteins that have the same molecular weight but differ in
their pI are best separated by
A. affinity chromatography.

19. The proteins EF-1 of eukaryotes and EF-Tu of bacteria are

similar in sequence and function. What can we conclude about the
relationship between EF-1 and EF-Tu?
A. that they are derived from different ancestors
B. that they are orthologs
C. that they are signature sequences
D. that they are paralogs
20. The titration curve of the amino acid glycine reveals a pK1 of
2.34, a pI of 5.97, and a pK2 of 9.60. When dissolved in water,
which ionic species is most likely to predominate at pH = 5.97?

B. size exclusion chromatography.

C. two-dimensional electrophoresis.
D. SDS polyacrylamide gel electrophoresis.
16. When an enzymatic activity is purified from a complex mixture

A.

of proteins what usually happens to total protein amount and

specific activity during the purification process?
A. Total protein amount and specific activity both increase.
B. Total protein amount and specific activity both decrease.
C. Total protein amount increases and specific activity

B.

decreases.
D. Total protein amount decreases and specific activity
increases.
17. Which of the following is true about the chemical synthesis of
peptides?
A. Peptides are synthesized on an insoluble support.

C.

C. Hsp70 is needed to stimulate the aggregation of proteins

denatured by heat.
D. Hsp70 is needed to protect proteins that have been
denatured by heat.
D.

6. A protein is in its native conformation when

Lehninger Biochemistry 4e Ch 04
1. X-ray diffraction and nuclear magnetic resonance (NMR), two
techniques used to solve the three-dimensional structure of

A. it is thermodynamically least stable.

B. it has the highest Gibbs free energy.

molecules, differ in that

C. it is in any of its functional, folded states.
A. NMR is limited to molecules that can be crystallized.
D. it is unfolded.
B. NMR is better for analyzing large proteins.
C. only molecules to be analyzed by NMR need to be labeled
with isotopes.
D. only x-ray diffraction is successful on all proteins.

7. Hydrogen bonds between amino acids in a polypeptide occur

between which chemical groups?
A. the C=O and C-H groups
B. the C=O and C-R groups

2. Which of the following poses a limitation on the size of proteins?

C. the C=O groups
A. the availability of amino acids
D. the C=O and N-H groups
B. a protein's conformation

8. Protein disulfide isomerase aids in the folding of proteins by

C. a protein's environment

A. shuffling hydrogen bonds between amino acids.

D. the error frequency during protein synthesis

B. reducing disulfide bonds between amino acids.

3. Which of the following experiments provided the first evidence

that the amino acid sequence of a polypeptide chain contains all the
information required to fold the chain into its native, threedimensional structure?
A. When ribonuclease is treated with urea, it loses its catalytic
activity.
B. When denatured ribonuclease is allowed to renature, it
regains its catalytic activity.
C. When renatured ribonuclease is allowed to denature, it

C. catalyzing the isomerization of cis and trans isomers of

amino acids.
D. shuffling disulfide bonds between amino acids.
9. Proline residues are most likely to occur in which of the following
secondary structures?
A. an -helix
B. a -turn
C. a -sheet

regains its catalytic activity.

D. a coiled coil
D. Addition of mercaptoethanol causes ribonuclease to regain

10. Fibrous proteins differ from globular proteins in that

catalytic activity.
4. Two or more proteins that have little sequence similarity, but
share the same major structural motif and have functional
similarities, belong to the same
A. fold.

A. fibrous proteins tend to serve structural functions, and

globular proteins are more likely to be enzymes.
B. fibrous proteins can often contain several types of
secondary structure, whereas globular proteins usually consist
largely of a single type of secondary structure.

B. family.
C. globular proteins are insoluble in water, and fibrous
C. superfamily.
D. motif.
5. The Hsp70 molecular chaperone proteins are more abundant in
cells stressed by elevated temperatures because
A. Hsp70 is needed to unfold proteins denatured by heat.
B. Hsp70 is needed to destroy proteins denatured by heat.

proteins are usually soluble.

D. globular proteins are more likely than fibrous proteins to
have an elaborate quaternary structure.
11. Why is the -helix conformation in polypeptides such a stable
form?
A. The -helix structure is stabilized by hydrophobic

interactions.
B. The -helix structure is stabilized by hydrogen bonds.
C. The -helix structure is stabilized by disulfide bonds.
D. The -helix structure is stabilized by proline residues.
12. In what way do the Hsp70 class and the chaperonin class of

16. Which bonds are planar (cannot rotate) in a polypeptide

backbone?
A. C-C bonds
B. C-N bonds
C. N-Cbonds

proteins differ from each other?

D. C-C bonds
A. Only the chaperonin class forms elaborate protein
complexes that contain a pocket into which unfolded proteins bind.
B. Only the chaperonin class requires ATP hydrolysis.

Lehninger Biochemistry 4e Ch 05
1. Which of the following is true about sickle-cell anemia?
A. People with sickle-cell anemia have inherited one or more
alleles for sickle-cell hemoglobin.

C. Only the Hsp70 class of proteins is present in higher

eukaryotes.

B. People with sickle-cell anemia have normal levels of

hemoglobin and normal numbers of erythrocytes.

D. The Hsp70 class will only help fold proteins under stress
conditions, whereas the chaperonin class will help fold proteins
under stress conditions and under normal conditions.

C. People with sickle-cell anemia have sickle-cell hemoglobin

molecules that form insoluble fibers.

13. Which of the following is true about the difference between

proteins with a rotational symmetry and proteins with a helical
symmetry?

D. People with sickle-cell anemia have a mutation in either

the or hemoglobin chains.
2. Which of the following is true about the structure of all

A. Virus coats, or capsids, can have only a rotational

immunoglobulins?

symmetry.
A. The chains are linked by disulfide bonds.
B. Icosahedral proteins have a helical symmetry rather than a
rotational symmetry.
C. Proteins with rotational symmetry tend to form a closed
structure, while proteins with helical symmetry tend to form an
open structure.
D. Proteins with rotational symmetry are less restricted in size
than those with a helical symmetry.
14. A protein in solution is more likely to maintain its native

B. They consist of two heavy chains and two light chains.

C. The five classes of immunoglobulins have a characteristic
type of light chain.
D. An antigen-binding site is formed by the combination of
two heavy chains.
3. Polyclonal antibodies
A. are produced by a population of identical B cells.

conformation when
B. are produced by different B cells, each responding to the
A. the number of hydrogen bonds within a protein is

same epitope within an antigen.

minimized.
C. are produced by different B cells, each responding to a
B. the shell of water becomes more ordered.
C. the protein is least stable.
D. its hydrophobic residues are largely buried in the protein
interior.
15. Which of the following is true about protein domains?
A. Protein domains lose their three-dimensional structure

different epitope within an antigen.

D. are produced by B cells grown in cell culture.
4. During skeletal muscle contraction, which of the following
narrows?
A. the I band
B. the Z disk

when separated from the remainder of the polypeptide chain.

C. the A band
B. Protein domains lose their function when separated from
the remainder of the polypeptide chain.

D. the M line
5. Which of the following is true about the role of ATP during

C. Protein domains often fold into stable globular units.

D. A protein must have more than one domain to be
functional.

skeletal muscle contraction?

A. After hydrolysis of ATP at the myosin head, Pi and ADP are
immediately released.

10M, all of the available insulin receptor sites are occupied.

B. The release of Pi from myosin is needed for the "power
stroke" that causes filament sliding.

D. It means that when the concentration of the insulin

receptor is 1 x 10-10M, all of the available insulin receptor sites are

C. Binding of ATP causes the myosin head to bind actin

filaments.
D. The hydrolysis of ATP at the myosin head causes myosin to
tightly bind the next actin subunit.
6. Which of the following is true about the organization of skeletal

occupied.
11. How does hemoglobin bind O2 cooperatively?
A. The binding of one molecule of O2 to one subunit of
hemoglobin enhances the assembly of other subunits to form a
complete hemoglobin protein.

muscle?
B. The binding of one molecule of O2 to one hemoglobin
A. Myofibrils consist of repeating sarcomeres.
B. Myofibrils consist of numerous muscle fibers.
C. The sarcoplasmic reticulum surrounds each muscle fiber.

protein enhances the binding of a molecule of O2 to a different

hemoglobin protein.
C. The binding of one molecule of O2 to one subunit of
hemoglobin enhances the affinity of the same subunit for more

D. Sarcomeres contain a complete I band and a complete A

molecules of O2.

band.
7. Which of the following is true about the difference between

D. The binding of one molecule of O2 to one subunit of

ELISA and immunoblot assays, both of which can be used to detect

hemoglobin enhances the affinity of other subunits for O2.

protein antigens?

12. What is the role of cytotoxic T cells (TC) in the immune

response?

A. Only immunoblots allow for quantification of the presence

of an antigen in a sample.

A. They produce cytokines and interleukins that stimulate the

proliferation of immune cells.

B. Only ELISA assays require a secondary antibody.

B. They produce immunoglobulins (antibodies) that bind
C. Only immunoblots enable an approximation of an antigen's

bacteria or viruses and target them for destruction.

molecular weight.
C. They destroy virally infected cells to which they are
D. Only ELISA assays require a purified protein antigen.

complexed through their T-cell receptors.

8. Which of the following is true about proteins and enzymes?

D. They ingest large particles and cells by phagocytosis.
A. All proteins bind ligands.
B. All enzymes have binding sites.

13. Vertebrates have MHC (major histocompatibility complex)

proteins that help the organism to distinguish self from non-self.
What is the difference between class I MHC proteins and class II

C. All proteins have active sites.

D. All enzymes are catalytic.
9. Which of the following binding constants has the highest affinity?
A. Ka = 1.0 x 107M-1
B. Kd = 1.0 x 10-9M
C. Kd = 1.5 x 10-9M

MHC proteins?
A. Only class II MHC proteins are found on the surface of
virtually all cells.
B. Only class I MHC proteins bind and display peptides
derived from cellular proteins.
C. Class I MHC proteins consist of one chain, and class II MHC
proteins consist of two chains.

D. Ka = 2.0 x 108M-1
10. The dissociation constant (Kd) of the human insulin receptor for
insulin is 1 x 10-10M. What does this mean?

D. Class I MHC proteins display peptides that can be

recognized by helper T cells (TH) and class II MHC proteins display
peptides that can be recognized by cytotoxic T cells (TC).

A. It means that when the concentration of insulin is 1 x 10-

14. What is the role of the heme prosthetic group in hemoglobin?

10M, half of the available insulin receptor sites are occupied.

A. The heme group coordinates the subunits of hemoglobin.
B. It means that when the concentration of the insulin
receptor is 1 x 10-10M, half of the available insulin receptor sites
are occupied.
C. It means that when the concentration of insulin is 1 x 10-

B. The heme group binds one molecule of oxygen in the

center of the hemoglobin protein.
C. The heme group binds a molecule of oxygen for each
subunit of hemoglobin.

Lehninger Biochemistry 4e Ch 06
D. The iron atom in the heme group is needed to irreversibly
bind oxygen.
15. Which of the following is true about the T (tense) R
(relaxed) transition of hemoglobin?

1. Which of the following is true about cofactors, which are

essential to the activity of some enzymes?
A. A holoenzyme is the protein part of an enzyme that is not
catalytically active until a cofactor is bound.

A. The T state of hemoglobin binds oxygen with a higher

affinity than the R state.
B. The binding of O2 to a subunit T state can cause the
transition of other subunits to the R state.
C. The T state has a narrower pocket between subunits than
does the R state.
D. When hemoglobin undergoes the T R transition, the
structures of the individual subunits change dramatically.
16. How do IgG antibodies lead to the destruction of viruses?
A. Virus-specific IgG antibodies coat the virus and deliver it to
macrophages for engulfment by phagocytosis.
B. Virus-specific antibodies coat the virus, causing the

B. Inorganic metal ions are examples of coenzymes.

C. Cofactors that are covalently bound to an enzyme protein
are called prosthetic groups.
D. All enzymes are proteins.
2. A simple plot of V0 versus [S] is superior to a double-reciprocal
plot (1/Vo versus 1/[S]) if you are trying to
A. determine Vmax.
B. detect allosteric regulation.
C. determine the type of inhibition.
D. determine the Km.

disruption of the virus.

C. Virus-specific IgG antibodies coat the virus and deliver it to
cytotoxic T cells (TC).
D. Virus-specific IgG antibodies induce viruses to undergo
apoptosis.
17. Which of the following is not a function of hemoglobin?
A. It delivers O2 to peripheral tissues.
B. It removes CO2 from peripheral tissues.
C. It delivers CO2 to the lungs.
D. It delivers H+ to peripheral tissues.
18. The Bohr effect, the effect of pH and CO2 concentration on the
binding and release of oxygen by hemoglobin, dictates that
A. oxygen binds hemoglobin better at low pH.
B. oxygen and H+ are bound at the same sites in hemoglobin.
C. the binding of CO2 is inversely related to the binding of
oxygen.
D. the binding of CO2 is inversely related to the binding of

3. In the double-reciprocal plot, increasing the concentration of

inhibitor
A. raises the Vmax.
B. lowers the Km / Vmax.
C. raises the Km / Vmax.
D. lowers the Km.
4. In competitive inhibition, increasing concentrations of the
inhibitor will have the following effect on the kinetics of the
enzyme:

H+.
19. What is the biological advantage to the sigmoidal binding curve

A. Km will decrease.

of hemoglobin for oxygen?

B. Vmax will stay the same.
A. It ensures that hemoglobin has a high affinity for oxygen.
C. The reaction will cease because the inhibitor binds
B. It allows hemoglobin to bind oxygen irreversibly.
C. It ensures that hemoglobin can bind oxygen only weakly.
D. It allows hemoglobin to shift between low and high
affinities for oxygen.

irreversibly.
D. Km / Vmax will stay the same.
5. Which of the following is true about zymogens?
A. Proproteins are one type of zymogen.

change (G) of a reaction.

B. Zymogens are inactivated by inhibitor proteins.
D. The difference between the energy levels of the ground
C. Zymogens are enzymatically inactive.
D. Zymogens cleave proteases.
6. Which of the following is true about the phosphorylation of

state and transition state is always negative.

11. In what way does the binding of a substrate by an enzyme
enhance catalysis?

proteins?

A. It increases the interaction of the substrate with water.

A. Proteins are usually phosphorylated at amino acids that

have hydroxyl group-containing side chains.

B. The binding energy of the enzyme-substrate interaction

lowers the activation energy.

B. Phosphorylation of proteins is catalyzed by phosphatases.

C. It increases the entropy between substrates.

C. Phosphoryation always activates enzymes.

D. The specificity in phosphorylation is conferred solely by the
amino acid to be phosphorylated.

D. The binding of a substrate prevents the enzyme from

changing conformation.
12. An enzyme with a high turnover number has

7. In feedback inhibition

A. a high Kcat.

A. an enzyme in a pathway inhibits one of the earlier enzymes

B. a low Km.

in the pathway.
C. a high Vmax.

B. an intermediate in a pathway inhibits one of the earlier

enzymes in the pathway.

D. a high Kcat/Km.
13. Which of the following is true about allosteric enzymes?

C. the initial substrate of a pathway inhibits one of the

enzymes in the pathway.

A. Allosteric enzymes are always multimeric.

D. the end product of a pathway inhibits one of the enzymes

in the pathway.

B. Regulatory sites (allosteric sites) on an allosteric enzyme

are always different from the catalytic site.

8. Which of the following enzymes fits in the class of enzymes

C. Allosteric enzymes always change the conformation of the

known as hydrolases?

active site in response to binding of an allosteric modulator.

A. hexokinase
D. Suicide inactivators are examples of allosteric modulators.
B. chymotrypsin

14. Which of the following is true about general acid-base

catalysis?

C. glycogen phosphorylase
A. It requires the ions of water.

D. triose phosphate isomerase

9. Which of the following is true about the role of enzymes in
catalyzing chemical reactions?

B. Amino acid side chains on enzymes can act as proton

donors or acceptors.

A. Enzymes alter the equilibrium of a reaction.

C. Often involves covalent bonds formed between a metal ion

and the substrate.

B. Enzymes are needed to catalyze only thermodynamically

unfavorable reactions.

D. It involves a transient covalent bond between the enzyme

and the substrate.

C. Enzymes enhance the rate of reactions.

D. Enzymes eliminate the activation energy of a reaction.
10. Which of the following is true about the free-energy changes
involved in reactions that favor the formation of product?

15. The steady state of an enzyme-catalyzed reaction is reached

when
A. the rate of appearance of product over time is constant.
B. the rate of enzyme-substrate formation is constant.

A. The ground state free energy of the product must be lower

than the ground state free energy of the substrate.

C. the concentration of enzyme-substrate complex equals the

concentration of product.

B. The activation energy is the difference between the

substrate and product ground state free energies.

D. the concentration of the enzyme-substrate complex is

constant over time.

C. Enzymes lower the overall free standard free-energy

Lehninger Biochemistry 4e Ch 07

water.

1. Based on the structures of Dglucose and Dgalactose (shown

B. Disaccharides form when a hydoxyl group of one

below), which of the following statements is true?

monosaccharide reacts with the hydroxyl group of another

monosaccharide.
C. A disaccharide consists of two monosaccharides linked to
each other by an N-glycosidic bond.
D. Disaccharides are formed by a hydrolysis reaction.
4. The reducing end of a disaccharide or a polysaccharide is
A. the end with an anomeric carbon that cannot be oxidized.
B. the end that does not have an anomeric carbon.
C. the end of a chain with a free anomeric carbon (i.e., not
involved in a glycosidic bond).
D. The end whose sugar cannot take the linear form.
5. Which of the following is a structural polysaccharide in plant
A. Glucose and galactose are ketoses.
B. Glucose and galactose are anomers of each other.
C. Glucose and galactose are tetroses.
D. Glucose and galactose are epimers of each other.

cells?
A. glycogen
B. amylose
C. starch
D. cellulose
6. Which of the following is true about proteoglycans?
A. They are small in size.
B. They are present in the extracellular matrix.
C. They comprise the cell wall of gram-positive bacteria.
D. They are glycolipids.
7. Why is glucose not stored in its monomeric form in cells?
A. Because monomeric glucose would raise the osmolarity of
the cytosol to unsafe levels.
B. Because the monomeric form of glucose is not very

2. Which of the following statements is true about the cyclic (ring)

form of Dglucose?
A. The cyclic form of Dglucose is a furanose.
B. The cyclic form of Dglucose involves the formation of a
covalent bond between the carbonyl group and the oxygen of a
hydroxyl group along the chain.

soluble.
C. Because the monomeric form of glucose cannot be readily
utilized as an energy source.
D. Because glucose monomers spontaneously form polymers
in the cell.
8. Which of the following is true about how sugar polymers are
broken down?

C. The cyclic form of Dglucose is the result of a bond forming

between the C1 and C6 carbon atoms.

A. Most animals cannot use starch as a fuel source because

they lack the enzyme to break it down.

D. In aqueous solution, the cyclic form of Dglucose is rare.

3. Which of the following is true about how a disaccharide is
formed from two monosaccharides?
A. Monosaccharides are linked in a reaction that eliminates

B. Starch and glycogen are broken down starting at the outer

branches.
C. When starch and glycogen are broken down for energy

production, glucose residues are removed from the reducing end.

C. Use a genetically engineered version of the cholera toxin
D. Glucose residues in starch and glycogen are removed in a

with an altered carbohydrate-binding site.

spontaneous condensation reaction.

D. Use a genetically engineered version of the cholera toxin

9. In starch and glycogen, the glucose monomers are joined by (1

4) linkages, whereas in cellulose, the glucose monomers are
joined by (1 4) linkages. What is a biological consequence of
this difference in sugar linkage?

lacking the carbohydrate-binding site as a vaccine to elicit an

immune response.
14. Treatment of gram-positive bacteria with penicillin will have
what effect?

A. Cellulose is generally not digestible by animals, whereas

starch is easily digestible.
B. Cellulose takes on a helical structure and starch forms

A. It will inhibit cell wall synthesis by hydrolyzing the (1 4)

bonds that connect the carbohydrate residues of the cell wall
peptidoglycan.

fibers.
C. Starch has more tensile strength than cellulose.

B. It will inhibit synthesis of lipopolysaccharides in the outer

membrane.
C. It will inhibit cell wall synthesis by preventing the synthesis

D. Glycogen is unbranched, while cellulose is highly branched.

10. In O-linked glycoproteins

of peptide cross-links in the cell wall peptidoglycan.

D. It will have no effect on gram-positive bacteria; it is

A. an oligosaccharide forms an O-glycosidic bond with an Asn

residue of the protein.

specific to gram-negative bacteria.

15. Which of the following is true about reducing ends?

B. an oligosaccharide forms an O-glycosidic bond between a

A. All polysaccharides have an equal number of reducing ends

residue on the protein and an OH group on the oligosaccharide.

C. an oligosaccharide forms an O-glycosidic bond with the -

as nonreducing ends.
B. Polysaccharides grow in the direction of the nonreducing

carbon on a residue of the protein.

end.
D. an oligosaccharide forms an O-glycosidic bond involving
the anomeric carbon of the oligosaccharide.
11. Lectins are
A. carbohydrates that can bind a protein.

C. Disaccharides are named starting with the reducing end.

D. All disaccharides have one reducing end. (see p. 249)
16. What role do lectins play in the infection of host cells by
influenza virus?

B. proteins linked to carbohydrates.

A. A plasma membrane lectin on the host cell binds the
C. proteins that bind carbohydrates.
D. the oligosaccharide moieties on glycoproteins.
12. In order to analyze the oligosaccharide moieties on a

carbohydrate moiety on an influenza virus glycoprotein.

B. Lectins present inside the cell target influenza viruses for
transfer to the lysosome.

glycoprotein, the first step is to cleave the oligosaccharides from

the protein by

C. An influenza virus lectin binds to the carbohydrate moiety

on glycoproteins on the host cell surface.

A. treatment with strong acid.

D. An influenza virus lectin binds to the carbohydrate moiety
B. treatment with endoglycosidase.
C. treatment with exoglycosidase.
D. treatment with a methylating agent.
13. Which is the safest and most effective way to develop a
vaccine that would protect the recipient if exposed to the natural
toxin of Vibrio cholerae, the bacterium that causes cholera.
A. Use purified natural toxin as a vaccine to elicit an immune
response.
B. Use live toxin-bearing Vibrio cholerae as a vaccine to elicit
an immune response.

on glycolipids on the host cell surface.