Biochemistry: Chapter 5 Exam
1. What is the primary function of myoglobin?
A) Enzyme regulation
B) Oxygen transport
C) Structural support
D) Signal transduction
2. What type of proteins are insulin and somatotropin classified as?
A) Structural proteins
B) Transport proteins
C) Effector proteins
D) Defense proteins
3. What phenomenon describes the process when a ligand induces a conformational
change in a protein?
A) Competitive binding
B) Induced-fit
C) Cooperative binding
D) Allosteric regulation
4. Which metal ion is crucial for the reversible binding of oxygen in heme proteins?
A) Mg²⁺
B) Cu²⁺
C) Fe²⁺
D) Zn²⁺
5. What happens to the color of heme when oxygen binds to it?
A) Changes from bright red to dark purple
B) Changes from dark purple to bright red
C) Remains unchanged
D) Changes to green
6. In the context of protein-ligand interactions, what does Kd represent?
A) The concentration at which all binding sites are occupied
B) The concentration of ligand at which half the binding sites are occupied
C) The ratio of bound to free protein
D) The strength of the bond between protein and ligand
7. The fraction of ligand-binding sites on the protein occupied by the ligand is
represented by which symbol?
A) Ka
B) Kd
C) θ (theta)
D) [PL]
8. What is the binding equilibrium expression for a protein (P) and ligand (L)?
A) P + L → PL
B) P + L ⇌ PL
C) PL → P + L
D) PL ⇌ P + L
9. At a very high concentration of ligand, which concentration remains constant?
A) [P]
B) [PL]
C) [L]
D) Ka
10. When the partial pressure of O2 is at [O2]0.5, it is referred to as:
A) Kd
B) P50
C) θ
D) Ka
11. What is the role of histidine (His) in heme binding?
A) It binds oxygen directly.
B) It prevents oxidation of iron.
C) It stabilizes the heme structure.
D) It is part of the porphyrin ring.
12. What type of protein is actin classified as?
A) Transport protein
B) Regulatory protein
C) Structural protein
D) Defense protein
13. Which of the following proteins is primarily involved in immune response?
A) Hemoglobin
B) Myoglobin
C) Immunoglobulins
D) Insulin
14. The equilibrium constant Ka reflects what aspect of the ligand-protein interaction?
A) Rate of ligand dissociation
B) Affinity of the ligand for the protein
C) Concentration of the ligand
D) Total binding sites available
15. What structural feature of heme allows it to bind oxygen?
A) Porphyrin ring structure
B) Sulfur atoms
C) Linear carbon chain
D) Hydrophobic pocket
16. How does CO binding affinity change when heme is part of myoglobin compared
to free heme?
A) It increases by 200 times.
B) It decreases by 200 times.
C) It remains unchanged.
D) It increases by 20,000 times.
17. Which protein is responsible for muscle contraction?
A) Collagen
B) Hemoglobin
C) Myosin
D) Ferritin
18. What type of motion involves collective motions of bonded and non-bonded
neighboring groups of atoms?
A) Atomic fluctuations
B) Large-scale conformational changes
C) Intermediate motions
D) None of the above
19. What physiological factor primarily influences the binding of oxygen to
myoglobin?
A) pH level
B) Temperature
C) Partial pressure of O2
D) Concentration of CO2
20. What role do weak forces play in protein structure?
A) They create strong covalent bonds.
B) They maintain higher order structure and allow flexibility.
C) They have no effect on protein structure.
D) They stabilize the protein completely.
21. What is the primary function of hemoglobin?
A) To transport nutrients
B) To carry O2 in the blood
C) To remove waste products
D) To regulate pH
22. At what concentration of carbon monoxide (CO) does a headache and dizziness
begin within six to eight hours of exposure?
A) 100 ppm
B) 200 ppm
C) 35 ppm
D) 400 ppm
23. What is the saturation percentage of hemoglobin in venous blood returning to the
lungs?
A) 96%
B) 64%
C) 50%
D) 80%
24. How long is the lifespan of red blood cells (RBCs)?
A) 60 days
B) 90 days
C) 120 days
D) 150 days
25. Myoglobin has a binding curve that is described as:
A) Sigmoid
B) Hyperbolic
C) Linear
D) Exponential
26. What type of protein is hemoglobin classified as?
A) Enzymatic protein
B) Structural protein
C) Allosteric protein
D) Transport protein
27. The T-state of hemoglobin is stabilized by:
A) Hydrogen bonds
B) Ionic bonds
C) Covalent bonds
D) Van der Waals forces
28. What happens to the heme porphyrin when O2 binds to hemoglobin?
A) It becomes puckered
B) It becomes more planar
C) It disintegrates
D) It remains unchanged
29. The Bohr effect describes the relationship between:
A) pH and hemoglobin affinity for O2
B) Temperature and oxygen binding
C) Pressure and hemoglobin structure
D) CO2 concentration and RBC lifespan
30. In the lungs, the pH of the blood is approximately:
A) 6.8
B) 7.2
C) 7.6
D) 8.0
31. What percentage of O2 saturation does hemoglobin have in arterial blood leaving
the lungs?
A) 50%
B) 64%
C) 80%
D) 96%
32. The Hill coefficient (nH) indicates:
A) The total number of binding sites
B) The degree of interaction between binding sites
C) The affinity of hemoglobin for CO2
D) The stability of the T-state
33. Sickle cell anemia is caused by a mutation in the:
A) α chain of hemoglobin
B) β chain of hemoglobin
C) Myoglobin structure
D) RBC membrane
34. What type of interactions stabilize the T-state of deoxyhemoglobin?
A) Hydrophobic interactions
B) Hydrogen bonds
C) Ionic interactions
D) Covalent interactions
35. Which molecule binds to the N-terminal end of each globin molecule in
hemoglobin?
A) O2
B) CO2
C) H+
D) Glucose
36. How many residues are in the α subunit of hemoglobin?
A) 141
B) 146
C) 120
D) 130
37. The transition from T-state to R-state in hemoglobin is triggered by:
A) Decrease in pH
B) Increase in temperature
C) Binding of O2
D) Release of CO2
38. The sigmoid O2-binding curve of hemoglobin allows for:
A) Efficient O2 release in tissues and loading in lungs
B) Constant O2 binding regardless of concentration
C) Inefficient transport of O2
D) Binding of CO2 instead of O2
39. The presence of which ion helps stabilize hemoglobin in its T-state?
A) Na+
B) K+
C) H+
D) Ca2+
40. How does the concentration of H+ affect hemoglobin's affinity for O2?
A) High H+ concentration increases affinity
B) Low H+ concentration decreases affinity
C) High H+ concentration decreases affinity
D) H+ concentration has no effect
ANSWER KEY
1. B) Oxygen transport
2. C) Effector proteins
3. B) Induced-fit
4. C) Fe²⁺
5. B) Changes from dark purple to bright red
6. B) The concentration of ligand at which half the binding sites are occupied
7. C) θ (theta)
8. B) P + L ⇌ PL
9. C) [L]
10. B) P50
11. B) It prevents oxidation of iron.
12. C) Structural protein
13. C) Immunoglobulins
14. B) Affinity of the ligand for the protein
15. A) Porphyrin ring structure
16. B) It decreases by 200 times.
17. C) Myosin
18. C) Intermediate motions
19. C) Partial pressure of O2
20. B) They maintain higher order structure and allow flexibility.
21. B) To carry O2 in the blood
22. C) 35 ppm
23. B) 64%
24. C) 120 days
25. B) Hyperbolic
26. C) Allosteric protein
27. B) Ionic bonds
28. B) It becomes more planar
29. A) pH and hemoglobin affinity for O2
30. C) 7.6
31. D) 96%
32. B) The degree of interaction between binding sites
33. B) β chain of hemoglobin
34. C) Ionic interactions
35. B) CO2
36. A) 141
37. C) Binding of O2
38. A) Efficient O2 release in tissues and loading in lungs
39. C) H+
40. C) High H+ concentration decreases affinity
