1. Max Perutz's investigation of the structure of hemoglobin primarily utilized_____.
   A
   Option A: mass spectrometry
   B
   Option B: genomics
   C
   Option C: NMR spectroscopy
   D
   Option D: X-ray crystallography
   E
   Option E: genetic engineering

Option D: X-ray crystallography

2. Hemerythrin and hemocyanin are:
   A
   Option A: hemoglobin variants that are found in animals at high altitude.
   B
   Option B: oxygen transport proteins found in invertebrates.
   C
   Option C: human mutant hemoglobins with decreased oxygen affinity.
   D
   Option D: synthetic derivatives of hemoglobin's heme group used in artificial blood substitutes.
   E
   Option E: tetrameric hemoglobin derivatives containing only α-chains (α4 tetramers).

Option B: oxygen transport proteins found in invertebrates.

3. Hemoglobin is a heterotetramer. How many protomers are present in hemoglobin?
   A
   Option A: 2
   B
   Option B: 1
   C
   Option C: 3
   D
   Option D: 0
   E
   Option E: 4

Option A: 2

4. The primary structure of mammalian hemoglobin, an α2 β2 tetramer, is approximately _____ identical to myoglobin.
   A
   Option A: 98%
   B
   Option B: 18%
   C
   Option C: 2%
   D
   Option D: 50%
   E
   Option E: 78%

Option B: 18%

5. Myoglobin and a single chain of hemoglobin have similar ______ structures.
   A
   Option A: tertiary
   B
   Option B: none of the above
   C
   Option C: secondary
   D
   Option D: primary
   E
   Option E: quaternary

Option A: tertiary

6. Carbon monoxide binds to heme:
   A
   Option A: in a manner that displaces carbon dioxide, causing CO2 poisoning.
   B
   Option B: with a higher affinity than oxygen.
   C
   Option C: resulting in the oxidation of the Fe(II) to Fe(III).
   D
   Option D: from the side opposite oxygen, resulting in a brown colored heme.
   E
   Option E: with a lower affinity than oxygen.

Option B: with a higher affinity than oxygen.

7. If the gene for myoglobin is "knocked out" in mice, the mice:
   A
   Option A: have their growth stunted.
   B
   Option B: respire extremely rapidly.
   C
   Option C: have larger lungs.
   D
   Option D: appear normal, with lighter colored muscle tissue.
   E
   Option E: have dark brown muscle tissue.

Option D: appear normal, with lighter colored muscle tissue.

8. Myoglobin's primary physiological role is to facilitate oxygen ________.
   A
   Option A: storage
   B
   Option B: binding
   C
   Option C: metabolism
   D
   Option D: reduction
   E
   Option E: diffusion

Option E: diffusion

9. Myoglobin's secondary structure is primarily composed of ______________.
   A
   Option A: parallel β-sheets
   B
   Option B: antiparallel β-sheets
   C
   Option C: Ω-loops
   D
   Option D: α-helices
   E
   Option E: polyproline helices

Option D: α-helices

10. Which of the following statements does not apply to the K value in the equation for the oxygen binding curve of myoglobin?
    A
    Option A: If Y > K, then myoglobin is less than 50% saturated with oxygen.
    B
    Option B: It is numerically equal to p50.
    C
    Option C: It is the value of pO2 at which Y = 0.5.
    D
    Option D: It is a measure of the affinity of myoglobin for oxygen.
    E
    Option E: It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied.

Option A: If Y > K, then myoglobin is less than 50% saturated with oxygen.