Protein Function Multiple Choice Questions

1-The interactions of ligands with proteins:

A) Are relatively nonspecific. B) Are relatively rare in biological systems.
C) Are usually irreversible. D) Are usually transient.

2-A prosthetic group of a protein is a non-protein structure that i

s:
A) a ligand of the protein.
B) a part of the secondary structure of the protein.
C) a substrate of the protein.
D) Permanently associated with the protein.
E) Transiently bound to the protein.

3-When oxygen binds to a hem-containing protein, the two open coordinati

on bonds of Fe2+ are occupied by:
A) One O atom and one amino acid atom.
B) One O2 molecule and one amino acid atom.
C) One O2 molecule and one heme atom.
D) Two O atoms.

4- Which of the following statements is correct?

(A) At 10 mm Hg partial pressure, hemoglobin binds oxygen but
myoglobin does not.
(B) At 20 mm Hg partial pressure, myoglobin and hemoglobin bind oxygen
in equal amounts.
(C) At 40 mm Hg partial pressure, myoglobin has a greater affinity
for oxygen than hemoglobin has.
(D) At 80 mm Hg partial pressure, myoglobin binds twice as much oxygen
as hemoglobin binds.

Both myoglobin and hemoglobin are proteins that bind reversibly with
molecular oxygen. The graph below shows the oxygen-binding saturation
of each protein at different
concentrations of oxygen

1
5. In
the binding of oxygen to myoglobin, the relationship between the conce
ntration of oxygen and the
fraction of binding sites occupied can best be described as:
A) Hyperbolic. B) Linear with a negative slope. C)
Linear with a positive slope.
D) Random. E) Sigmoidal.

6. Myoglobin and the subunits of hemoglobin have:

A) No obvious structural relationship.
B) Very different primary and tertiary structures.
C) Very similar primary and tertiary structures.
D) Very similar primary structures, but different tertiary
structures.
E) Very similar tertiary

7. An allosteric interaction between a ligand and a protein is one in which:

A) Binding of a molecule to a binding site affects binding of additional
molecules to the same site.
B) Binding of a molecule to a binding site affects binding properties
of another site on the protein.
C) Binding of the ligand to the protein is covalent.
D) Multiple molecules of the same ligand can bind to the same binding
site.
E) Two different ligands can bind to the same binding site.

8. In hemoglobin, the transition from T state to R state (low to high

affinity) is triggered by:
A) Fe 2+ binding B) heme binding. C) Oxygen binding.
D) Subunit association. E) Subunit dissociation.

9. Which of the following is not correct concerning 2,3-

bisphosphoglycerate (BPG)y structures, but different primary structures.
A) It binds at a distance from the heme groups of hemoglobin.
B)
It binds with lower affinity to fetal hemoglobin than to adult hemoglobin.
C) It increases the affinity of hemoglobin for oxygen.
D) It is an allosteric modulator.
E)
It is normally found associated with the hemoglobin extracted from red bl
ood cells.

10. The fundamental cause of sickle-

cell disease is a change in the structure of:
A) Blood. B) Capillaries. C) Hemoglobin. D) Red cells. E)
The heart

2
11. Allosteric effects that occur in hemoglobin
Only occur in humans.
Are important for maintaining Fe in the Fe2+ state.
Minimize oxygen delivery to the tissues.
Optimize oxygen delivery to the tissues.

12. The cooperativity of O2 binding to hemoglobin results in a

100-fold higher affinity for the last O2 bound than for the first.
100-fold lower affinity for the last O2 bound than for the first.
Extensive protein conformational change.
Release of H+ with the dissociation of O2.
The first and third choices are both correct.

13. Spontaneous oxidation of the heme-bound Fe(II) to Fe(III) is prevented

in hemoglobin by
a. The symmetry of its quaternary structure.
B. The four heme-protein covalent bonds.
c. A highly-ordered water molecule within the heme pocket.
d. The surrounding protein structure in each subunit.

14 In sickle cell anemia, the basis of the malfunction of the

hemoglobin molecule is:
a. Incorrect secondary structure. B. Substitution of a single
amino acid.
c. Faulty binding of the heme groups. D. Reduced affinity for
oxygen.

15. Most oxygen carried in the blood is:

a. In solution with the plasma
b. Combined with plasma proteins
c. Chemically combined with a heme group
d. Carried as HCO3-

16. Which statement about CO2 is incorrect?

a. Its concentration in the blood is decreased by hyperventilation
b. Its accumulation in the blood is associated with a drop in pH
c. More CO2 dissolves in the blood plasma than is carried on RBCs
d. [CO2]VENOUS is greater than [CO2]ARTERIAL

17. Most CO2 is transported in the blood in the form of:

a. Dissolved gas
b. Carbaminohemoglobin
c. Bicarbonate ion
d. Carboxyhemoglobin

18. Oxygen is transported by red blood cells by binding to:

3
A) Specific receptors on the plasma membrane.
B) Specific receptors within the nucleus of the red blood cell.
C) The beta polypeptide chain of the globin portion of hemoglobin.
D) The polypeptide chain of the heme portion of hemoglobin.
E) The iron ion in the heme portion of hemoglobin.

19 The binding of oxygen to hemoglobin is characterized as:

a. Compliant Irreversible Reversible Noncompliant

20. To say that hemoglobin is fully saturated means that:

A) The red blood cells contain as many hemoglobin molecules as possible.

B) Oxygen is attached to both the heme and the globin portions of the
molecule.
C) It is carrying both oxygen and carbon dioxide simultaneously.
D) Some molecule other than oxygen is attached to the oxygen binding
sites on hemoglobin.
E) There is an oxygen molecule attached to each of the four heme
groups.

21. Which of the following would be TRUE if the oxygen-hemoglobin

dissociation curve is shifted to the right?
A) Partial pressure of carbon dioxide is increased.
B) pH is increased. C) Temperature is decreased.
D) Levels of BPG are decreased. E) Partial pressure of oxygen is
decreased.

22. BPG is a substance that:

A) is responsible for the detergent activity of surfactant.
B) catalyzes the conversion of carbon dioxide to bicarbonate ion.
C) is produced during glycolysis in erythrocytes and increases the
dissociation of oxygen from hemoglobin.
D) inhibits the activity of the central chemoreceptors to prolong
inspiration.
E) binds extra oxygen onto fetal hemoglobin.

23. Hemoglobin will tend to bind more oxygen at a given partial

pressure of oxygen if:
A) The partial pressure of carbon dioxide is increased.
B) the temperature is increased.
C) The pH is increased.
D) BPG concentration increases.
E) the concentration of hydrogen ions increases.

24. High partial pressure of carbon dioxide favors the formation

of:
A) BPG. B) Carbaminohemoglobin. C) Chloride ions. D)
Oxyhemoglobin.

4
25. Carbonic acid is produced when:
A) Oxygen combines with bicarbonate ion.
B) Carbon dioxide combines with bicarbonate ion.
C) Carbon dioxide combines with water.
D) Oxygen and carbon dioxide combine.
E) Carbon dioxide attached to hemoglobin.

26. Hemoglobin:
(a) combines preferentially with O2 over any other substance.
(b) when combined with carbon dioxide is known as carboxyhemoglobin.
(c) plays a critical role in determining the amount of O2 that is
exchange between alveoli and blood, because it acts as a storage
depot, removing dissolved O2 from diffusion of O2 to continue
until the hemoglobin is completely saturated.
(d) Both (b) and (c) above are correct.
(e) All of the above are correct.

27. Carbonic anhydrase:

(a) Is found in the red blood cells.
(b) Catalyzes the formation of carbonic acid from carbonic dioxide and
water.
(c) Catalyzes the formation of oxyhemoglobin from oxygen and reduce
hemoglobin
(d) Both (a) and (b) above are correct.
(e) Both (a) and (c) above are correct.
28) 2, 3-diphosphoglycerate:
(a) Is produced within red blood cells.
(b) Production is inhibited increases whenever HbO2.
(c) Concentration gradually increases whenever Hb in the arterial blood is
chronically under saturated.
(d) Both (a) and (b) above are correct.
(e) All of the above are correct.