a) hyperbolic b) linear c) sigmoidal d) electrostatic e) none of the above 46·Th

Question

a) hyperbolic b) linear c) sigmoidal d) electrostatic e) none of the above 46·The oxygen binding curve of the myoglobin protein is best described as: a) hyperbolic b) linear c) sigmoidal d) electrostatic e) none of the above 47. In the protein hemoglobin, HI 46 of the subunit interacts with D94 of the subunit. Which of the following best describes this interaction interaction/tertiary structure a) hydrophobic b) hydrophobic interaction/quaternary structure c) electrostatic i d) electrostatic interaction/tertiary structure e) electrostatic interaction/quaternary structure 48. The oxygen binding curve of the hemoglobin stripped of BPG is best described as: a) hyperbolic b) linear c) sigmoidal d) electrostatic e) none of the above 49. Sicle Cell Anemia is caused by mutation in the gene that encodes for which of the following subunits of bemoglobin? a) b) c) d) e) co

Explanation / Answer

46. The correct answer is hyperbolic, i.e. option a.

Explanation: Haemoglobin exists in two conformations - a high-affinity R state and a low-affinity T state. When oxygen concentration levels are high, as in the lungs, the R state is favored, enabling the maximum amount of oxygen to be bound to the hemes. In the capillaries, where oxygen concentration levels are lower, the T state is favored, in order to facilitate the delivery of oxygen to the tissues.The Bohr effect is dependent on this allostery, as increases in CO2 and H+ help stabilize the T state and ensure greater oxygen delivery to muscles during periods of elevated cellular respiration. This is evidenced by the fact that myoglobin, a monomer with no allostery, does not exhibit the Bohr effect. Hence, the oxygen binding curve of the myoglobin protein is hyperbolic.

47. The correct answer is electrostatic interaction/quaternary structure, i.e. option e.

48. The correct answer is sigmoidal, i.e. option c.

Here, 2,3-BPG binds to a pocket in the T-state of hemoglobin and is released as it forms the R-state. The presence of 2,3-BPG means that more oxygen must be bound to the hemoglobin before the transition to the R-form is possible.

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