All of the following are considered "weak" interactions in proteins, except:

A) hydrogen bonds.
B) hydrophobic interactions.
C) ionic bonds.
D) peptide bonds.
E) van der Waals forces.
D
The most important contribution to the stability of a protein's
conformation appears to be the:

A) entropy increase from the decrease in ordered water molecules forming
a solvent shell around it.
B) maximum entropy increase from ionic interactions between the ionized
amino acids in a protein.
C) sum of free energies of formation of many weak interactions among the
hundreds of amino acids in a protein.
D) sum of free energies of formation of many weak interactions between its
polar amino acids and surrounding water.
E) stabilizing effect of hydrogen bonding between the carbonyl group of
one peptide bond and the amino group of another.
A
In an aqueous solution, protein conformation is determined by two major
factors. One is the formation of the maximum number of hydrogen bonds.
The other is the:

A) formation of the maximum number of hydrophilic interactions.
B) maximization of ionic interactions.
C) minimization of entropy by the formation of a water solvent shell
around the protein.
D) placement of hydrophobic amino acid residues within the interior of the
protein.
E) placement of polar amino acid residues around the exterior of the
protein.
D
Pauling and Corey's studies of the peptide bond showed that:

A) at pH 7, many different peptide bond conformations are equally
probable.
B) peptide bonds are essentially planar, with no rotation about the CN
axis.
C) peptide bonds in proteins are unusual, and unlike those in small model
compounds.
D) peptide bond structure is extraordinarily complex.
E) primary structure of all proteins is similar, although the secondary and
tertiary structure may differ greatly.
B
the plane drawn behind the peptide bond indicates the (drawn behind the
peptide bond)

A) absence of rotation around the CN bond because of its partial
double-bond character.
B) plane of rotation around the CN bond.
C) region of steric hindrance determined by the large C=O group.
D) region of the peptide bond that contributes to a Ramachandran plot.
E) theoretical space between -180 and +180 degrees that can be occupied
by the and angles in the peptide bond.
A
Which of the following best represents the backbone arrangement of two
peptide bonds?

A) CNCCCNCC
B) CNCCNC
C) CNCCCN
D) CCNCCN
E) CCCNCCC
D
Which of the following pairs of bonds within a peptide backbone show free
rotation around both bonds?

A) CC and NC
B) C=O and NC
C) C=O and NC
D) NC and CC
E) NC and NC
A
Roughly how many amino acids are there in one turn of an helix?

A) 1
B) 2.8
C) 3.6
D) 4.2
E) 10
C
In the alpha helix the hydrogen bonds:

F) are roughly parallel to the axis of the helix.
G) are roughly perpendicular to the axis of the helix.
H) occur mainly between electronegative atoms of the R groups.
I) occur only between some of the amino acids of the helix.
J) occur only near the amino and carboxyl termini of the helix.
A
In an helix, the R groups on the amino acid residues:

A) alternate between the outside and the inside of the helix.
B) are found on the outside of the helix spiral.
C) cause only right-handed helices to form.
D) generate the hydrogen bonds that form the helix.
E) stack within the interior of the helix.
B
Thr and/or Leu residues tend to disrupt an helix when they occur next to
each other in a protein because:

A) an amino acids like Thr is highly hydrophobic.
B) covalent interactions may occur between the Thr side chains.
C) electrostatic repulsion occurs between the Thr side chains.
D) steric hindrance occurs between the bulky Thr side chains.
E) the R group of Thr can form a hydrogen bond.
D
A D-amino acid would interrupt an helix made of L-amino acids.
Another naturally occurring hindrance to the formation of an helix is
the presence of:

A) a negatively charged Arg residue.
B) a nonpolar residue near the carboxyl terminus.
C) a positively charged Lys residue.
D) a Pro residue.
E) two Ala residues side by side.
D
An helix would be destabilized most by:

A) an electric dipole spanning several peptide bonds throughout the
helix.
B) interactions between neighboring Asp and Arg residues.
C) interactions between two adjacent hydrophobic Val residues.
D) the presence of an Arg residue near the carboxyl terminus of the
helix.
E) the presence of two Lys residues near the amino terminus of the helix.
E
The major reason that antiparallel -stranded protein structures are more
stable than parallel -stranded structures is that the latter:

A) are in a slightly less extended configuration than antiparallel strands.
B) do not have as many disulfide crosslinks between adjacent strands.
C) do not stack in sheets as well as antiparallel strands.
D) have fewer lateral hydrogen bonds than antiparallel strands.
E) have weaker hydrogen bonds laterally between adjacent strands.
E
Amino acid residues commonly found in the middle of turn are:

A) Ala and Gly.
B) hydrophobic.
C) Pro and Gly.
D) those with ionized R-groups.
E) two Cys.
C
A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-
Gly-. The sequence is most probably part of a(n):

A) antiparallel sheet.
B) parallel sheet.
C) helix.
D) sheet.
E) turn.
E
The three-dimensional conformation of a protein may be strongly
influenced by amino acid residues that are very far apart in sequence. This
relationship is in contrast to secondary structure, where the amino acid
residues are:

A) always side by side.
B) generally near each other in sequence.
C) invariably restricted to about 7 of the 20 standard amino acids.
D) often on different polypeptide strands.
E) usually near the polypeptide chain's amino terminus or carboxyl
terminus.
B
The -keratin chains indicated by the diagram below have undergone one
chemical step (S-S to SH SH). To alter the shape of the -keratin chains
as in hair wavingwhat subsequent steps are required?

A) Chemical oxidation and then shape remodeling
B) Chemical reduction and then chemical oxidation
C) Chemical reduction and then shape remodeling
D) Shape remodeling and then chemical oxidation
E) Shape remodeling and then chemical reduction
D
Which of the following statements is false?

A) Collagen is a protein in which the polypeptides are mainly in the -helix
conformation.
B) Disulfide linkages are important for keratin structure.
C) Gly residues are particularly abundant in collagen.
D) Silk fibroin is a protein in which the polypeptide is almost entirely in
the conformation.
E) -keratin is a protein in which the polypeptides are mainly in the -
helix conformation.
A
Kendrew's studies of the globular myoglobin structure demonstrated that:

A) "corners" between -helical regions invariably lacked proline residue.
B) highly polar or charged amino acid residues tended to be located
interiorally.
C) myoglobin was completely different from hemoglobin, as expected.
D) the structure was very compact, with virtually no internal space
available for water.
E) the helix predicted by Pauling and Corey was not found in myoglobin.
D
Determining the precise arrangement of atoms within a large protein is
possible only through the use of:

A) electron microscopy.
B) light microscopy.
C) molecular model building.
D) Ramachandran plots.
E) x-ray diffraction.
E
Analysis of x-ray diffraction data yields a(n) ; analysis of 2D NMR data
yields a(n) .

A) electron density map; count of hydrogen atoms in the molecule
B) shadow of protein's outline; estimate of protein's molecular volume
C) table of interatomic distances; electron density map
D) electronic density map; table of interatomic distances
E) 3-d protein structure; 2-d protein structure
D
Proteins often have regions that show specific, coherent patterns of folding
or function. These regions are called:

A) domains.
B) oligomers.
C) peptides.
D) sites.
E) subunits.
A
Which of the following statements concerning protein domains is true?

A) They are a form of secondary structure.
B) They are examples of structural motifs.
C) They consist of separate polypeptide chains (subunits).
D) They have been found only in prokaryotic proteins.
E) They may retain their correct shape even when separated from the rest
of the protein.
E
The structural classification of proteins (based on motifs) is based
primarily on their:

A) amino acid sequence.
B) evolutionary relationships.
C) function.
D) secondary structure content and arrangement.
E) subunit content and arrangement.
D
Proteins are classified within families or superfamilies based on
similarities in:

A) evolutionary origin.
B) physico-chemical properties.
C) structure and/or function.
D) subcellular location.
E) subunit structure.
C
Which of the following statements about oligomeric proteins is false?

A) A subunit may be similar to other proteins.
B) All subunits must be identical.
C) Many have regulatory roles.
D) Some oligomeric proteins can further associate into large fibers.
E) Some subunits may have nonprotein prosthetic groups.
B
A repeating structural unit in a multimeric protein is known as a(n):

A) domain.
B) motif.
C) oligomer.
D) protomer.
E) subunit.
D
Which of the following statements concerning rotational symmetry in
proteins is false?

A) It involves rotation of proteins inside the cell.
B) It is frequently seen in the subunits of oligomeric proteins.
C) It is frequently seen in viruses.
D) It may involve rotation about one or more axes.
E) It results in closed, packed structures.
A
An average protein will not be denatured by:

A) a detergent such as sodium dodecyl sulfate.
B) heating to 90C.
C) iodoacetic acid.
D) pH 10.
E) urea.
C
Which of the following is least likely to result in protein denaturation?

A) Altering net charge by changing pH
B) Changing the salt concentration
C) Disruption of weak interactions by boiling
D) Exposure to detergents
E) Mixing with organic solvents such as acetone
B
Experiments on denaturation and renaturation after the reduction and
reoxidation of the SS bonds in the enzyme ribonuclease (RNase)
have shown that:

A) folding of denatured RNase into the native, active conformation,
requires the input of energy in the form of heat.
B) native ribonuclease does not have a unique secondary and tertiary
structure.
C) the completely unfolded enzyme, with all SS bonds broken, is
still enzymatically active.
D) the enzyme, dissolved in water, is thermodynamically stable relative to
the mixture of amino acids whose residues are contained in RNase.
E) the primary sequence of RNase is sufficient to determine its specific
secondary and tertiary structure.
E
Which of the following statements concerning the process of spontaneous
folding of proteins is false?

A) It may be an essentially random process.
B) It may be defective in some human diseases.
C) It may involve a gradually decreasing range of conformational species.
D) It may involve initial formation of a highly compact state.
E) It may involve initial formation of local secondary structure.
A
Protein S will fold into its native conformation only when protein Q is also
present in the solution. However, protein Q can fold into its native
conformation without protein S. Protein Q, therefore, may function as a
____________ for protein S.

A) ligand
B) molecular chaperone
C) protein precursor
D) structural motif
E) supersecondary structural unit
B
Which of the following is not known to be involved in the process of
assisted folding of proteins?

A) Chaperonins
B) Disulfide interchange
C) Heat shock proteins
D) Peptide bond hydrolysis
E) Peptide bond isomerization
D
Any given protein is characterized by a unique amino acid sequence
(primary structure) and three-dimensional (tertiary) structure. How are
these related?
Ans: The three-dimensional structure is determined by the amino acid sequence. This means that the amino
acid sequence contains all of the information that is required for the polypeptide chain to fold up into a
discrete three-dimensional shape.
Name four factors (bonds or other forces) that contribute to stabilizing the
native structure of a protein, and describe one condition or reagent that
interferes with each type of stabilizing force.
Ans: Among forces that stabilize native protein structures are (a) disulfide bonds, (b) hydrogen bonds, (c)
hydrophobic interactions, and (d) ionic interactions. Agents that interfere with these forces are (a)
mercaptoethanol or dithiothreitol, (b) pH extremes, (c) detergents and urea, and (d) changes in pH or ionic
strength, respectively.
When a polypeptide is in its native conformation, there are weak
interactions between its R groups. However, when it is denatured there are
similar interactions between the protein groups and water. What then
accounts for the greater stability of the native conformation?
Ans: In the unfolded polypeptide, there are ordered solvation shells of water around the protein groups. The
number of water molecules involved in such ordered shells is reduced when the protein folds, resulting in
higher entropy. Hence, the lower free energy of the native conformation.
Draw the resonance structure of a peptide bond, and explain why there is
no rotation around the
CN bond.
Ans: The intermediate resonance structure imparts a partial double bond characteristic to the CN bond,
thereby prohibiting rotation. (See Fig. 4-2, p. 116.)
Pauling and Corey showed that in small peptides, six atoms associated
with the peptide bond all lie in a plane. Draw a dipeptide of two amino
acids in trans linkage (side-chains can be shown as R), and indicate
which six atoms are part of the planar structure of the peptide bond.
Ans: The N and H of the amino and the C and O of the carbonyl are all in the same plane with the two C
atoms, which are diagonally opposite relative to the CN bond. (See Fig. 4-2, p. 119.)
Draw the hydrogen bonding typically found between two residues in an
helix.
Ans: Hydrogen bonds occur between every carbonyl oxygen in the polypeptide backbone and the peptide
NH of the fourth amino acid residue toward the amino terminus of the chain. (See Fig. 4-2, p. 116.)
Describe three of the important features of the -helical polypeptide
structure predicted by Pauling and Corey. Provide one or two sentences
for each feature.
Ans: The -helical structure of a polypeptide is tightly wound around a long central axis; each turn of the
right-handed helix contains 3.6 residues and stretches 5.4 along the axis. The peptide NH is hydrogen-
bonded to the carbonyl oxygen of the fourth amino acid along the sequence toward the amino terminus.
The R groups of the amino acid residues protrude outward from the helical backbone.
Describe three of the important features of a sheet polypeptide structure.
Provide one or two sentences for each feature.
Ans: In the sheet structure, several extended polypeptides, or two regions of the same polypeptide, lie
side by side and are stabilized by hydrogen bonding between adjacent chains. Adjacent chains may be
either parallel (with a repeat distance of about 6.5 ) or antiparallel (7 repeat). The R groups are often
small and alternately protrude from opposite faces of the sheet.
Why are glycine and proline often found within a turn?
Ans: A turn results in a tight 180 reversal in the direction of the polypeptide chain. Glycine is the
smallest and thus most flexible amino acid, and proline can readily assume the cis configuration, which
facilitates a tight turn.
Explain how circular dichroism spectroscopy could be used to measure the
denaturation of a protein.
Ans: Circular dichroism spectroscopy measures the amount of -helix in a given protein. As the protein
denatures, the amount of -helix should decrease as the protein chain becomes disordered; this change
would be detectable using CD spectrography.
In superhelical proteins, such as collagen, several polypeptide helices are
intertwined. What is the function of this superhelical twisting?
Ans: The superhelical twisting of multiple polypeptide helices makes the overall structure more compact
and increases its overall strength.
Why is silk fibroin so strong, but at the same time so soft and flexible?
Ans: Unlike collagen and keratin, silk fibroin has no covalent crosslinks between adjacent strands, or
between its stacked sheets, making it very flexible. Fibroin's unusual tensile strength derives from the fact
that the peptide backbone of antiparallel -strands is fully extended, and that the R-groups in the stacked
pleated sheets interdigitate, preventing any longitudinal sliding of the sheets across one another.
What is typically found in the interior of a water-soluble globular protein?
Ans: Hydrophobic amino acid residues cluster away from the surface in globular proteins, so much of the
protein's interior is a tightly packed combination of hydrocarbon and aromatic ring R groups with very few
water molecules.
How does one determine the three-dimensional structure of a protein?
Your answer should be more than the name of a technique.
Ans: The protein is crystallized, and the crystal structure is determined by x-ray diffraction. The pattern of
diffracted x-rays yields, by Fourier transformation, the three-dimensional distribution of electron density.
By matching electron density with the known sequence of amino acids in the protein, each region of
electron density is identified as a single atom. Sometimes, the three-dimensional structure of a small protein
or peptide can be determined in solution by sophisticated analysis of the NMR spectrum of the polypeptide.
This technique can also reveal dynamic aspects of protein structure such as conformational changes.
Computer analysis of two-dimensional NMR spectra can be used to generate a picture of the three-
dimensional structure of a protein.
Describe a reservation about the use of x-ray crystallography in
determining the three-dimensional structures of biological molecules.
Ans: To obtain an x-ray picture of a biomolecule, the molecule must be purified and crystallized under
laboratory conditions far different from those encountered by the native molecule. Biomolecules in the cell
also have more flexibility and freedom of motion than can be accommodated in a rigid crystal structure.
Therefore, the static picture obtained from an x-ray analysis of a crystal may not provide a complete or
accurate representation of the biomolecule in vivo.
Explain what is meant by motifs in protein structure.
Ans: Motifs are particularly stable arrangements of elements of secondary structure (e.g., helix and
conformation), including the connections between them, which are found in a variety of proteins.
Draw a loop, and describe what is found in the interior of the loop.
Ans: Hydrophobic amino acid residues are usually found in the interior of the loop; these help stabilize the
arrangement through hydrophobic interactions. (See Fig. 4-20, p. 140.)
Describe the quaternary structure of hemoglobin.
Ans: Each protein molecule is composed of two copies each of two different subunits and . The two
protomers are arranged with C2 symmetry.
Describe briefly the two major types of symmetry found in oligomeric
proteins and give an example of each.
Ans: 1) Rotational: In rotational symmetry, subunits are superimposable after rotation about one or more of
the axes. Some examples are hemoglobin and thepoliovirus capsid. 2) Helical: In helical symmetry,
subunits are superimposable after a helical rotation. Some examples are actin filaments and the tobacco
mosaic virus capsid.
What is the rationale for many large proteins containing multiple copies of
a polypeptide subunit?
Ans: Each different polypeptide requires a separate gene that must be replicated and transcribed. It is
therefore more efficient to have fewer genes, encoding shorter polypeptides that can be used to construct
many large proteins.
Explain (succinctly) the theoretical and/or experimental arguments in
support of this statement: "The primary sequence of a protein determines
its three-dimensional shape and thus its function."
Ans: Anfinsen showed that a completely denatured enzyme (ribonuclease) could fold spontaneously into its
native, enzymatically active form with only the primary sequence to guide it.
Each of the following reagents or conditions will denature a protein. For
each, describe in one or two sentences what the reagent/condition does to
destroy native protein structure.

(a) urea
(b) high temperature
(c) detergent
(d) low pH
Ans: (a) Urea acts primarily by disrupting hydrophobic interactions. (b) High temperature provides thermal
energy greater than the strength of the weak interactions (hydrogen bonds, electrostatic interactions,
hydrophobic interactions, and van der Waals forces, breaking these interactions. (c) Detergents bind to
hydrophobic regions of the protein, preventing hydrophobic interactions among several hydrophobic
patches on the native protein. (d) Low pH causes protonation of the side chains of Asp, Glu, and His,
preventing electrostatic interactions.
How can changes in pH alter the conformation of a protein?
Ans: Changes in pH can influence the extent to which certain amino acid side chains (or the amino and
carboxyl termini) are protonated. The result is a change in net charge on the protein, which can lead to
electrostatic attractions or repulsions between different regions of the protein. The final effect is a change in
the protein's three-dimensional shape or even complete denaturation.
Once a protein has been denatured, how can it be renatured? If
renaturation does not occur, what might be the explanation?
Ans: Because a protein may be denatured through the disruption of hydrogen bonds and hydrophobic
interactions by salts or organic solvents, removal of those conditions will reestablish the original aqueous
environment, often permitting the protein to fold once again into its native conformation. If the protein does
not renature, it may be because the denaturing treatment removed a required prosthetic group, or because
the normal folding pathway requires the presence of a polypeptide chain binding protein or molecular
chaperone. The normal folding pathway could also be mediated by a larger polypeptide, which is then
cleaved (e.g., insulin). Denatured insulin would not refold easily.
What are two mechanisms by which "chaperone" proteins assist in the
correct folding of polypeptides?
Ans: Chaperones protect unfolded polypeptides from aggregation by binding to hydrophobic regions. They
can also provide a microenvironment that promotes correct folding.
Humans maintain a nearly constant level of hemoglobin by continually
synthesizing and degrading it. This is an example of a(n):

A)dynamic steady state.
B)equilibrium state.
C)exergonic change.
D) free-energy change
E) waste of energy
A
A true statement about hydrophobic interactions is that they:

A)are the driving force in the formation of micelles of amphipathic
compounds in water.
B)do not contribute to the structure of water-soluble proteins.
C)have bonding energies of approximately 20-40 Kjoule per mole.
D)involve the ability of water to denature proteins.
E)primarily involve the effect of polar solutes on the entropy of aqueous
systems.
A
Which of the following is true about the properties of aqueous solutions?

A)A pH change from 5.0 to 6.0 reflects an increase in the hydroxide ion
concentration ([OH-]) of 20%.
B)A pH change from 8.0 to 6.0 reflects a decrease in the proton
concentration ([H+]) by a factor of 100.
C)Charged molecules are generally insoluble in water.
D)Hydrogen bonds form readily in aqueous solutions.
E)The pH can be calculated by adding 7 to the value of the pOH.
D
The Henderson-Hasselbalch equation:

A)allows the graphic determination of the molecular weight of a weak acid
from its pH alone.
B)does not explain the behavior of di- or tri-basic weak acids
C)employs the same value for pKa for all weak acids.
D)is equally useful with solutions of acetic acid and of hydrochloric acid.
E)relates the pH of a solution to the pKa and the concentrations of acid
and conjugate base.
E
Consider an acetate buffer, initially at the same pH as its pKa (4.76). When
sodium hydroxide (NaOH) is mixed with this buffer, the:

A)pH remains constant.
B)pH rises more than if an equal amount of NaOH is added to an acetate
buffer initially at pH 6.76.
C)pH rises more than if an equal amount of NaOH is added to unbuffered
water at pH 4.76.
D)ratio of acetic acid to sodium acetate in the buffer falls.
E)sodium acetate formed precipitates because it is less soluble than acetic
acid.
D
The chirality of an amino acid results from the fact that its carbon:

A)has no net charge.
B)is a carboxylic acid.
C)is bonded to four different chemical groups.
D)is in the L absolute configuration in naturally occurring proteins.
E)is symmetric.
c
Of the 20 standard amino acids, only ___________ is not optically active.
The reason is that its side chain ___________.

A) alanine; is a simple methyl group
B) glycine; is a hydrogen atom
C) glycine; is unbranched
D) lysine; contains only nitrogen
E) proline; forms a covalent bond with the amino group
b
Two amino acids of the standard 20 contain sulfur atoms. They are:
A) cysteine and serine.
B) cysteine and threonine.
C) methionine and cysteine
D) methionine and serine
E) threonine and serine.
c
All of the amino acids that are found in proteins, except for proline,
contain a(n):
A) amino group.
B) carbonyl group.
C) carboxyl group.
D) ester group.
E) thiol group.
a
The three-dimensional structure of macromolecules is formed and
maintained primarily through noncovalent interactions. Which one of the
following is not considered a noncovalent interaction?

A) carbon-carbon bonds
B) hydrogen bonds
C) hydrophobic interactions
D) ionic interactions
E) van der Walls interactions
a
Amino acids are ampholytes because they can function as either a(n):

A) acid or a base.
B) neutral molecule or an ion.
C) polar or a nonpolar molecule.
D) standard or a nonstandard monomer in proteins.
E) transparent or a light-absorbing compound
a
For amino acids with neutral R groups, at any pH below the pI of the
amino acid, the population of amino acids in solution will have:

A) a net negative charge.
B) a net positive charge.
C) no charged groups.
D) no net charge.
E) positive and negative charges in equal concentration.
b
Which of the following statements about buffers is true?

A) A buffer composed of a weak acid of pKa = 5 is stronger at pH 4 than at
pH 6.
B) At pH values lower than the pKa, the salt concentration is higher than
that of the acid.
C) The pH of a buffered solution remains constant no matter how much
acid or base is added to the solution.
D) The strongest buffers are those composed of strong acids and strong
bases.
E) When pH = pKa, the weak acid and salt concentrations in a buffer are
equal.
e
The formation of a peptide bond between two amino acids is an example of
a(n) ______________ reaction.

A) cleavage
B) condensation
C) group transfer
D) isomerization
E) oxidation reduction
b
What is the advantage of adding SDS to gel electrophoresis?
A) SDS colors the proteins for visualization.
B) SDS reduces disulfide bonds.
C) SDS allows proteins to be separated on the basis of approximate mass.
D) None of the above.
E) All of the above.
c
Two-dimensional electrophoresis is a combination of what two techniques?
A) isoelectric focusing and affinity chromatography
B) ion-exchange chromatography and SDS-PAGE
C) affinity chromatography and SDS-PAGE
D) isoelectric focusing and SDS-PAGE
E) isoelectric focusing and ion-exchange chromatography
d
Trypsin cleaves the peptide bond at
A) the carboxyl side of Arg and Lys residues
B) the carboxyl side of Met residues
C) the amino acid terminus
D) none of the above
E) all of the above
a
Cyanogen bromide cleaves the peptide bond at
A) the carboxyl side of Arg and Lys residues
B) the carboxyl side of Met residues
C) the amino acid terminus
D) none of the above
E) all of the above
b
Energy requiring metabolic pathways that yield complex molecules from
simpler precursors are:

A) amphibolic.
B) anabolic.
C) autotrophic.
D) catabolic.
b
If the free energy change G for a reaction is -46.11 kJ/mol, the reaction
is:

A) at equilibrium.
B) endergonic.
C) endothermic.
D) exergonic.
b
Which of the following describes the Bohr Effect?
A) Lowering the pH results in the release of O2 from oxyhemoglobin.
B) Increasing the pressure of CO2 results in the release of O2 from
oxyhemoglobin.
C) Increasing the pH increases the T-form of hemoglobin.
D) All of the above.
E) a and b
e
Which is not correct concerning the models that are accepted to describe
cooperative binding?
A) In the sequential model, the binding of a ligand changes the
conformation of the subunit to which it binds, which in turn induces a
change in neighboring subunits.
B) All known allosteric proteins exhibit either the concerted or sequential
model exclusive of the other.
C) Both models incorporate a low affinity T-state and a higher affinity R-
state.
D) Both models explain the sigmoid-shaped binding curve.
E) In the concerted model, all molecules exist either in the T-state or the R-
state.
b
What would be the expected result of a Lys residue being substituted with
a Ser residue in the BPG binding site of hemoglobin?
A) BPG would bind tighter because of the loss of a positive charge.
B) BPG would bind tighter because of the gain of a positive charge.
C) BPG would bind less tightly because of the loss of a positive charge
BPG would bind less tightly because of the gain of a positive charge.
This substitution would have no effect on the binding of BPG.
c
Hemoglobin-binding of oxygen is best described as a
A) concerted model.
B) Michaelis-Menten model.
C) sequential model.
D) combination of sequential and concerted models.
E) None of the above.
d
Which of the following is not correct concerning myoglobin?
A) The globin chain contains an extensive -helix structure.
B) The heme group is bound to the globin chain by two disulfide bonds to
cysteine residues
C) The iron of the heme group is in the Fe+2 oxidation state.
D) The diameter of the iron ion decreases upon binding to oxygen.
E) The function of myoglobin is oxygen storage in muscle.
b
Which of the following is correct concerning the differences between
hemoglobin and myoglobin?
A) Both hemoglobin and myoglobin are tetrameric proteins.
B) Hemoglobin exhibits a hyperbolic O2 saturation curve while myoglobin
exhibits a sigmoid shaped curve.
C) Hemoglobin exhibits cooperative binding of O2 while myoglobin does
not.
D) Hemoglobin exhibits a higher degree of O2 saturation at all
physiologically relevant partial pressures of O2 than does myoglobin.
E) All of the above.
c
Changes in ATCase conformation were detected by crystallizing the
enzyme in the presence of PALA (N-(phosphonacetyl)-L-aspartate). What
is PALA?
A) a radioactive tag that binds to the subunits
B) a bi-substrate analog that resembles the catalytic transition-state
intermediate
C) a fluorescent substrate analog
D) All of the above.
E) None of the above.