Hemoglobin & Transport of O2 & CO2

Include drawings, equations, graphs, etc. where appropriate.

1. Define the following: prosthetic group, fractional saturation, allosterism, cooperativity, Bohr effect, isohydric carriage, respiratory acidosis & alkalosis, metabolic acidosis & alkalosis. Please provide examples.

2. Describe the interactions (e.g., H-bonding) that are involved in the tight binding of heme to apomyoglobin?

3. Describe Myoglobin's structure (include comments on its primary, secondary, tertiary and quaternary structure).

4. What are the major similarities and differences in structure and properties between myoglobin and hemoglobin? Provide descriptions.

5. What are the structural & functional aspects of the effect of H+ on the O2 binding of hemoglobin? Include any pKa differences, at least one example of a specific functional group involved, etc. What are the consequences of this binding? How does it effect the body in the lungs and in the periphery?