Chapter 7: Protein Function Part I: Myoglobin and

Hemoglobin
Matching
A)
B)
C)
D)
E)
F)
G)
H)
I)
J)
K)
L)
M

positively cooperative
cyanosis
His E7
decrease
R
hydrogen bonds
increase
symmetry
His F8
ion pairs
T
hemolytic anemia
sequencial

1. When oxygen binds to heme, the oxygen forms a hydrogen bond with ______.
Ans: C
Level of Difficulty: Moderate
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
2. In the ______ state of hemoglobin, the iron ion is out of the plane of the porphyrin ring.
Ans: K
Level of Difficulty: Easy
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
3. The conversion of hemoglobin from the T to the R state requires breaking of ______
involving C-terminal residues.
Ans: J
Level of Difficulty: Easy
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

4. Hemoglobin's subunits bind oxygen in a ______ manner.

Ans: A
Level of Difficulty: Easy
Section: 7.1.C
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
5. An increase in pCO2 causes hemoglobin's affinity for oxygen to ______.
Ans: D
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
6. The absence of 2,3-BPG causes hemoglobin's affinity for oxygen to______.
Ans: G
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
7. The ______ model of allosterism requires subunits to change conformation simultaneously.
Ans: H
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
8. Sickle cell hemoglobin does not form fibers in the ______ form.
Ans: E
Level of Difficulty: Easy
Section: 7.1.E
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

9. When unstable hemoglobin is degraded; degradation products often cause cell lysis, leading
to a condition called ______.
Ans: L
Level of Difficulty: Moderate
Section: 7.1.E
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
10. Mutations that favor the oxidation of the heme iron(II) to iron(III) can cause ______.
Ans: B
Level of Difficulty: Moderate
Section: 7.1.E
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

Multiple Choice
11. Which of the following is not a ligand to the porphyrin ring Fe(II) ion in oxymyoglobin?
A) His E7
B) His F8
C) Nitrogen atoms in the porphyrin ring
D) Oxygen
E) all are ligands
Ans: A
Level of Difficulty: Moderate
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
12. Which gas does not bind to the porphyrin ring Fe(II) ion in myoglobin?
A) NO
B) CO
C) CO2
D) O2
E) H2S
Ans: C
Level of Difficulty: Easy
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
13. Which of the following statements does not apply to the K value in the equation for the
oxygen binding curve of myoglobin?
A) It is numerically equal to p50.
B) It is defined as that oxygen partial pressure at which half of the oxygen binding sites are
occupied.
C) It is a measure of the affinity of myoglobin for oxygen.
D) If Y > K, then myoglobin is less than 50% saturated with oxygen.
E) It is the value of pO2 at which Y = 0.5.
Ans: D
Level of Difficulty: Easy
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

14. Myoglobins secondary structure is primarily composed of ______________.

A) parallel -sheets
B) antiparallel -sheets
C) -helices
D) -loops
E) polyproline helices
Ans: C
Level of Difficulty: Easy
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
15. Myoglobins primary physiological role is to facilitate oxygen ________.
A) storage
B) metabolism
C) binding
D) reduction
E) diffusion
Ans: E
Level of Difficulty: Easy
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
16. If the gene for myoglobin is "knocked out" in mice, the mice:
A) have larger lungs.
B) respire extremely rapidly.
C) have dark brown muscle tissue.
D) appear normal, with lighter colored muscle tissue.
E) have their growth stunted.
Ans: D
Level of Difficulty: Moderate
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

17. Carbon monoxide binds to heme:

A) with a higher affinity than oxygen.
B) resulting in the oxidation of the Fe(II) to Fe(III)
C) in a manner that displaces carbon dioxide, causing CO2 poisoning.
D) from the side opposite oxygen, resulting in a brown colored heme.
E) with a lower affinity than oxygen.
Ans: A
Level of Difficulty: Easy
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
18. Myoglobin and a single chain of hemoglobin have similar ______ structures.
A) primary
B) secondary
C) tertiary
D) quaternary
E) none of the above
Ans: C
Level of Difficulty: Easy
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
19. The primary structure of mammalian hemoglobin, an 22 tetramer, is approximately _____
identical to myoglobin.
A) 2%
B) 18%
C) 50%
D) 78%
E) 98%
Ans: B
Level of Difficulty: Moderate
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

20. Hemoglobin is a heterotetramer. How many protomers are present in hemoglobin?

A) 0
B) 1
C) 2
D) 3
E) 4
Ans: C
Level of Difficulty: Easy
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
21. What is the type of symmetry that relates the protomers in hemoglobin with respect to each
other?
A) C2
B) C4
C) D2
D) D4
E) Tetrahedral symmetry
Ans: A
Level of Difficulty: Easy
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
22. Hemerythrin and hemocyanin are:
A) human mutant hemoglobins with decreased oxygen affinity.
B) hemoglobin variants that are found in animals at high altitude.
C) synthetic derivatives of hemoglobins heme group used in artificial blood substitutes.
D) oxygen transport proteins found in invertebrates.
E) tetrameric hemoglobin derivatives containing only -chains (4 tetramers).
Ans: D
Level of Difficulty: Easy
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

23. Max Perutzs investigation of the structure of hemoglobin primarily utilized_____.

A) X-ray crystallography
B) NMR spectroscopy
C) genomics
D) mass spectrometry
E) genetic engineering
Ans: A
Level of Difficulty: Easy
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
24. The oxygen binding by hemocyanins is mediated by
A) an iron ion
B) a pair of iron ions
C) a heme group
D) a copper atom
E) a pair of copper atoms
Ans: E
Level of Difficulty: Difficult
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
25. When the partial pressure of O2 in venous blood is 30 torr, the saturation of myoglobin with
O2 is ______ while the saturation of hemoglobin with O2 is ______.
A) 0.55, 0.91
B) 0.91, 0.55
C) 2.8 torr, 26 torr
D) 0.91, 0.97
E) none of the above
Ans: B
Level of Difficulty: Difficult
Section: 7.1.C
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

26. Hemoglobin's p50 value is about ______ as great as myoglobin's p50 value.
A) one-tenth
B) half
C) twice
D) ten times
E) twenty times
Ans: D
Level of Difficulty: Moderate
Section: 7.1.C
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
27. The value of n, the Hill constant (coefficient), for hemoglobin is about ______ as great as
the value for myoglobin.
A) half
B) twice
C) three times
D) five times
E) ten times
Ans: C
Level of Difficulty: Moderate
Section: 7.1.C
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
28. Consider a hypothetical hemoglobin-like molecule with a Hill coefficient (constant) of 1 and
the same p50 value as normal hemoglobin. Choose the statement below that best describes the
two proteins.
A) There is a cooperative interaction between oxygen-binding sites in both the hypothetical and
normal hemoglobins.
B) The hypothetical hemoglobin has a greater oxygen affinity than normal hemoglobin.
C) The oxygen binding curve for the hypothetical hemoglobin is hyperbolic, and the curve for
normal hemoglobin is sigmoidal.
D) The two hemoglobins would be able to deliver about the same amount of oxygen to the
tissues.
E) At pO2 less than p50, normal hemoglobin has a greater YO2 value.
Ans: C
Level of Difficulty: Moderate
Section: 7.1.C
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

29. The Hill plot shows that the fourth oxygen binds to hemoglobin with a ______-fold greater
affinity than the first.
A) 2
B) 5
C) 10
D) 20
E) 100
Ans: E
Level of Difficulty: Moderate
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
30. While the binding of O2 to myoglobin as a function of pO2 is described by a simple
__________ curve, the binding to hemoglobin is described by a more complex ______ curve.
A) sigmoidal; hyperbolic
B) hyperbolic; sigmoidal
C) exponential; hyperbolic
D) sigmoidal; bell-shaped
E) hyperbolic; concave
Ans: B
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
31. The Bohr effect refers to
A) the decrease in affinity of Hb for O2 when the pH goes down
B) the decrease in affinity of Hb for O2 when the pH goes up
C) the increase in the affinity of Hb for O2 when the O2 concentration goes up
D) the decrease in affinity of Hb for O2 when the BPG concentration goes up
E) the decrease in affinity of Hb for O2 when the BPG concentration goes down
Ans: A
Level of Difficulty: Easy
Section: 7.1.C
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

10

32. Which of the following increases the affinity of hemoglobin for O2?
A) an increase in BPG concentration
B) the formation of N-terminal carbamates
C) an increase in pH
D) a decrease in pH
E) an increase in CO2 concentration
Ans: C
Level of Difficulty: Moderate
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
33. The most rapid way that erythrocytes adapt to high altitudes is
A) by producing genetically altered hemoglobins that have higher O2-binding affinities.
B) by adopting the symmetry model of allosterism.
C) by increasing the concentration of hemoglobin.
D) by relying upon the simpler protein myoglobin.
E) by increasing the intracellular concentration of BPG.
Ans: E
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
34. The rearrangement of T state hemoglobin to the R state
A) occurs in each protein subunit independently when its heme binds oxygen.
B) requires the binding of at least three oxygen molecules.
C) increases the ion pairing interactions of the C-terminal amino acids.
D) involves the movement of the Fe(II) into the heme plane.
E) opens a central cavity for BPG binding.
Ans: D
Level of Difficulty: Moderate
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

11

35. Which of the following statements about the symmetry model of allosterism is not true?
A) the protein is an oligomer of symmetrically (or pseudosymmetrically) related subunits.
B) the oligomer can exist in two conformational states, which are in equilibrium.
C) the ligand can bind to a subunit in either conformation.
D) the molecular symmetry of the protein is conserved during the conformational change.
E) none of the above.
Ans: E
Level of Difficulty: Moderate
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
36. BPG stands for
A) biphenylglycine.
B) boronylphenylglutamate.
C) bisphosphoglycerate.
D) bisphenylglycerol.
E) betapropylglutamine.
Ans: C
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
37. Why is the decreased affinity of fetal hemoglobin for BPG advantageous?
A) With fewer BPG molecules bound there are more heme residues available for O2 binding.
B) Decreased BPG binding biases the fetal hemoglobin toward the R state.
C) More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state.
D) BPG is available to bind to fetal myoglobin, helping to release O2 in fetal muscle tissue.
E) none of the above
Ans: B
Level of Difficulty: Difficult
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

12

38. The reaction of carbonic anhydrase catalyzes

A) the formation of carbamates with the concomitant release of protons.
B) the hydration of bicarbonate, resulting in the formation of carbonic acid.
C) the reduction of carbon dioxide with the concomitant consumption of protons.
D) the hydration of carbon dioxide, forming bicarbonate and protons.
E) the hydrolysis of carbamates with the concomitant consumption of protons.
Ans: D
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
39. During the T to R conformational shift, Fe(II) drags the F-helix via a bond to the side chain
of ________.
A) Leu F7
B) Leu F4
C) His F8
D) Leu FG3
E) Val FG5
Ans: C
Level of Difficulty: Easy
Section: 7.1.D
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
40. Some abnormal hemoglobins have Hill coefficients that are ______ that of normal
hemoglobin, indicating that their ability to bind oxygen cooperatively has been compromised.
A) less than
B) greater than
C) much greater than
D) about equal to
E) The correct answer cannot be determined from the information given.
Ans: A
Level of Difficulty: Moderate
Section: 7.1.E
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

13

41. In sickle-cell anemia, the negatively charged glutamic acid residue is replaced by the neutral
amino acid ____________.
A) tyrosine
B) lysine
C) valine
D) adenosine
E) glycine
Ans: C
Level of Difficulty: Moderate
Section: 7.1.E
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
42. Hemoglobin S, the variant responsible for the misshapen red blood cells characteristic of the
disease sickle-cell anemia, is potentially advantageous to heterozygotes because it confers some
level of resistance to the disease _________.
A) rickets
B) AIDS
C) cyanosis
D) polycythemia
E) malaria
Ans: E
Level of Difficulty: Easy
Section: 7.1.E
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
43. ______of the worlds human population carries an inherited variant hemoglobin gene.
A) 5%
B) 25%
C) 50%
D) 75%
E) 90%
Ans: A
Level of Difficulty: Easy
Section: 7.1.E

14

Learning objective: Oxygen Binding to Myoglobin and Hemoglobin44. The repeating

functional unit in a myofibril is called
A) the A band.
B) the I band.
C) the sarcomere.
D) the H zone.
E) the M disk.
Ans: C
Level of Difficulty: Easy
Section: 7.2.A
Learning objective: Muscle Contraction
45. Muscle contraction is directly caused by
A) structural changes in actin.
B) structural changes in myosin.
C) structural changes in the A band.
D) structural changes in the Z disk.
E) None of the above is correct.
Ans: E
Level of Difficulty: Moderate
Section: 7.2.A
Learning objective: Muscle Contraction
46. Muscle contraction is directly caused by
A) structural changes in actin.
B) structural changes in myosin.
C) thick and thin filaments sliding past each other.
D) structural changes in the Z disk.
E) None of the above is correct.
Ans: C
Level of Difficulty: Easy
Section: 7.2.A
Learning objective: Muscle Contraction

15

47. Which of the statements about muscle contraction is correct?

A) During muscle contraction the sarcomere becomes shorter.
B) During muscle contraction the I band becomes shorter.
C) During muscle contraction the H zone becomes shorter.
D) During muscle contraction the distance between the Z disk and the M disk becomes shorter.
E) All of the answers above are correct.
Ans: E
Level of Difficulty: Moderate
Section: 7.2.A
Learning objective: Muscle Contraction
48. Which of the statements about muscle contraction is not true?
A) During muscle contraction the sarcomere becomes shorter.
B) During muscle contraction the I band becomes shorter.
C) During muscle contraction the H zone becomes shorter.
D) During muscle contraction the A band becomes shorter
E) During muscle contraction the distance between the Z disk and the M disk becomes shorter.
Ans: D
Level of Difficulty: Moderate
Section: 7.2.A
Learning objective: Muscle Contraction
49. What are the main bonds or forces that stabilize the dimer formed by two myosin heavy
chains?
A) hydrophobic interactions
B) hydrogen-bonds
C) ionic interactions
D) disulfide bonds
E) isopeptide bonds
Ans: A
Level of Difficulty: Easy
Section: 7.2.A
Learning objective: Muscle Contraction

16

50. During muscle contraction

A) myosin pulls actin filaments toward the M disk.
B) myosin pushes actin filaments toward the Z disk.
C) actin pulls myosin toward the Z disk.
D) actin pushes myosin toward the M disk.
E) All of the answers above are correct.
Ans: A
Level of Difficulty: Easy
Section: 7.2.A
Learning objective: Muscle Contraction
51. Which statement about myosin is not true?
A) Myosin is a heterohexamer.
B) Myosin contains two globular heads.
C) Myosin contains six different polypeptides
D) Myosin aggregates to form thick filaments
E) All of the answers above are true of myosin.
Ans: E
Level of Difficulty: Easy
Section: 7.2.A
Learning objective: Muscle Contraction
52. Which statement about actin is not true?
A. There are two actin genes, one for F-actin and one for G-actin.
B. Monomeric G-actin polymerizes to form F-actin.
C. Actin filaments are polar (the ends can be distinguished).
D. Actin can bind ATP.
E. Actin is a common protein in nonmuscle cells.
Ans: A
Level of Difficulty: Moderate
Section: 7.2.A
Learning objective: Muscle Contraction

17

53. The energy needed to drive muscle contraction comes from ATP hydrolysis that is carried
out by
A) G-actin.
B) F-actin.
C) myosin heads.
D) myosin tails.
E) tropomyosin.
Ans: C
Level of Difficulty: Easy
Section: 7.2.B
Learning objective: Muscle Contraction
54. During muscle contraction myosin heads
A) walk along thick filaments toward the M disk.
B) walk along thick filaments toward the Z disk.
C) walk along thin filaments toward the M disk.
D) walk along the thin filaments toward the H zone.
E) walk along the thin filaments toward the Z disk.
Ans: E
Level of Difficulty: Moderate
Section: 7.2.B
Learning objective: Muscle Contraction
55. Muscle contraction is triggered
A) in response to an increase in the cytoplasmic Ca2+ concentration.
B) in response to a decrease in the cytoplasmic Ca2+ concentration.
C) in response to an increase in the cytoplasmic cAMP concentration.
D) in response to a decrease in the cytoplasmic cAMP concentration.
E) in response to an increase in the cytoplasmic titin concentration.
Ans: A
Level of Difficulty: Moderate
Section: 7.2.B
Learning objective: Muscle Contraction

18

56. Which statement about actin is correct?

A) Actin is expressed only in muscle.
B) Actin is expressed at low levels in most cells.
C) No known function has been described for actin in nonmuscle cells.
D) Nonmuscle cells only contain G actin.
E) Actin is the most abundant cytoplasmic protein in many cell types.
Ans: E
Level of Difficulty: Moderate
Section: 7.2.C
Learning objective: Muscle Contraction
57. Which of the following statements about actin is not true?
A) Actin is the most abundant cytoplasmic protein in many cell types.
B) Actin forms microfilaments in many cell types.
C) Actin plays an important role in endocytosis.
D) Actin is present only as monomers in nonmuscle cells.
E) Actin filaments are dynamic, they grow at one end and they lose subunits at the other end.
Ans: D
Level of Difficulty: Moderate
Section: 7.2.C
Learning objective: Muscle Contraction
58. Treadmilling refers to
A) myosin heads walking along actin microfilaments.
B) actin and myosin filaments sliding along each other.
C) actin monomers moving through a microfilament from the + end to the end.
D) synthesis and degradation of actin monomers.
E) the interactions between actin and tropomyosin.
Ans: C
Level of Difficulty: Moderate
Section: 7.2.C
Learning objective: Muscle Contraction

19

59. Humoral immunity refers to that part of the immune response that is mediated by
A) T lymphocytes.
B) antibodies.
C) antigens.
D) the thymus.
E) the skin.
Ans: B
Level of Difficulty: Easy
Section: 7.3.A
Learning objective: Antibodies
60. Humoral immunity is mediated by soluble molecules. Which cell type produces the soluble
molecules that carry out the humoral immunity?
A) T cells
B) B cells
C) macrophages
D) neutrophils
E) monocytes
Ans: B
Level of Difficulty: Easy
Section: 7.3.A
Learning objective: Antibodies
61. How many different classes of antibodies are produced by the human immune system?
A) 1
B) 2
C) 3
D) 4
E) 5
Ans: E
Level of Difficulty: Easy
Section: 7.3.A
Learning objective: Antibodies

20

62. IgG is the most common immunoglobulin in the circulatory system and in the extravascular
fluid. It is composed of two light chains and two heavy chains. What is the approximate
molecular mass of an IgG molecule?
A) 23 kDa
B) 75 kDa
C) 150 kDa
D) 360 kDa
E) 950 kDa
Ans: C
Level of Difficulty: Moderate
Section: 7.3.A
Learning objective: Antibodies
63. IgG is one of five classes of antibodies that can be produced by our immune system. IgGs
have a molecular mass of approximately 150 kDa, what is their subunit composition?
A) 2 light chains and 2 heavy chains
B) 2 light chains, 2 heavy chains, and a J chain
C) 4 light chains, 4 heavy chains, and a J chain
D) 6 light chains, 6 heavy chains, and a J chain
E) 10 light chains, 10 heavy chains , and a J chain.
Ans: A
Level of Difficulty: Easy
Section: 7.3.A
Learning objective: Antibodies
64. Which class of antibodies has been implicated in allergic reactions?
A)
B)
C)
D)
E)

IgA
IgD
IgE
IgG
IgM

Ans: C
Level of Difficulty: Moderate
Section: 7.3.A
Learning objective: Antibodies

21

65. How many antigen-binding sites are present on an IgG molecule?

A) 1
B) 2
C) 3
D) 4
E) 5
Ans: B
Level of Difficulty: Easy
Section: 7.3.A
Learning objective: Antibodies
66. How many antigen-binding sites are present on an IgM molecule?
A) 2
B) 4
C) 10
D) 16
E) 25
Ans: C
Level of Difficulty: Moderate
Section: 7.3.A
Learning objective: Antibodies
67. Fab fragments can be generated by
A) reduction of IgG molecules.
B) oxidation of IgG molecules.
C) limited digestion of IgG molecules with papain.
D) combining two light chains.
E) combining two heavy chains.
Ans: C
Level of Difficulty: Moderate
Section: 7.3.A
Learning objective: Antibodies

22

68. Which statement about antigen-binding sites in antibodies is false?

A) An antigen-binding site on an IgG is formed by the amino-terminal ~110 amino acids of a
light chain and the amino terminal ~110 amino acids of a heavy chain.
B) An antigen-binding site on an IgG is formed by the variable region of a light chain and the
variable region of a heavy chain.
C) The antigen-binding site is composed of two Ig folds.
D) Antigen-binding specificity is determined by the sequences of the hypervariable sequences in
both the light chain and the heavy chain.
E) Antigen binding specificity is determined exclusively by the sequences in the carboxyterminal ~110 amino acids in the light chain and the heavy chain.
Ans: E
Level of Difficulty: Moderate
Section: 7.3.B
Learning objective: Antibodies
69. The Ig fold can be described as a
A) globular fold composed of helices.
B) a globular fold composed of a four helix bundle.
C) a globular fold composed of a sandwich.
D) a globular fold composed of barrel.
E) a coiled-coil.
Ans: C
Level of Difficulty: Moderate
Section: 7.3.B
Learning objective: Antibodies

23

SHORT ANSWER
70. Myoglobin is an oxygen binding protein in muscle. Describe in one sentence the overall
structure of myoglobin.
Ans: Myoglobin is a globular protein composed of 8 helices that forms a hydrophobic pocket
that contains the heme group.
Level of Difficulty: Moderate
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
71. What is the primary physiological function of myoglobin in most mammals?
Ans: The primary physiological function of myoglobin in most mammals is to increase the
solubility for O2 in muscle tissue and thereby increasing the diffusion rate.
Level of Difficulty: Moderate
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
72. It appears that the heme group in myoglobin binds the O2. What is the function of the
polypeptide?
Ans: The polypeptide performs various functions: 1. The polypeptide provides solubility for
the heme group, which is very non-polar. 2. The polypeptide prevents permanent oxidation of
the Fe(II). 3. The polypeptide helps coordinate the Fe(II) (His F8) 4. The polypeptide forms a
H-bond with the O2 (His E7).
Level of Difficulty: Difficult
Section: 7.1.A
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin
73. Mammals and other animals have a circulatory system because diffusion is to slow to supply
the tissues with oxygen in animals that are larger than 2 millimeter. Explain in one sentence why
these circulatory systems contain hemoglobin or other oxygen binding proteins?
Ans: Oxygen-binding proteins increase the solubility of oxygen in the fluid of the circulatory
system. This is important because oxygen is not very soluble in aqueous solutions.
Level of Difficulty: Difficult
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

24

74. The graph below shows the O2-binding curves for myoglobin (Mb) and hemoglobin (Hb).
a. Label the two curves (indicate which one represents Mb and which one represents Hb).

b. Use the graph to determine the Kd of myoglobin for O2 (show your approach).
c. What is the difference between myoglobin and hemoglobin that cause the O2-binding curves
to so be different?
d. Why is it important that hemoglobin has these particular O2-binding characteristics?

Ans: a. See graph.

b. Kd equals 3-4 torr (see graph).
c. Mb has one subunit, Hb has 4 subunits. The sigmoid binding curve is a consequence of
positive cooperativity between the 4 O2-binding sites in Hb. The hyperbolic binding curve for
myoglobin is the result of oxygen binding reaction being noncooperative.
d. As a consequence of positive cooperation Hb has a high affinity for O2 when the O2
concentration is high (in the lungs) and low affinity for O2 when the O2 concentration is low (in
the tissues). As a consequence Hb binds large amount of O2 in the lungs and releases large
amounts of O2 in the tissues, resulting in efficient transport of O2.
Level of Difficulty: Difficult
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

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75. You have been studying O2 binding to a hemerythrin-like protein isolated from an exotic
marine worm. Your O2-binding data are shown in the table below.
a. Use the data to generate an O2-binding curve (do not forget to mark the axes).
b. Use the curve to estimate the Kd for the interaction.
c. Is there any evidence from your data that this hemoglobin-like protein binds O2 in a
cooperative manner (briefly explain your answer)?
[Ligand] in M
21
42
79
118
257
362
535
745
900
1052

Y
0.11
0.28
0.37
0.42
0.58
0.66
0.78
0.86
0.89
0.92

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Ans: a. see curve

b. see curve, Kd equals 180 M
c. there is no evidence for cooperative binding of O2 to this protein, because the binding curve is
hyperbolic and not sigmoid.
Level of Difficulty: Difficult
Section: 7.1.B
Learning objective: Oxygen Binding to Myoglobin and Hemoglobin

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