Reading Guide, Stryer Short Course, Chapter 9
1.Draw an oxygen binding curve of hemoglobin and myoglobin. Label the axes. Use it to explain why hemoglobin is better at transporting oxygen from the lungs to the tissues. (Fig 9.2)
2. What is the physiological role of myoglobin?
3. What is a heme group? What occupy the fifth and sixth coordination sites of the heme?
4. What is the purpose of the distal histidine?
5. Describe the quaternary structure of hemoglobin.
6. Deoxyhemoglobin corresponds to the __________________ of hemoglobin and oxyhemoglobin corresponds to the __________________.
7. In a short essay, explain the structural basis of hemoglobin oxygen binding cooperativity.
8. What is the role of 2,3-bisphosphoglycerate (2,3-bPG) in hemoglobin oxygen binding? If no 2,3-bPG is present, hemoglobin’s binding curve looks like the binding curve of _________________.
9. How is fetal hemoglobin different than adult hemoglobin? Why?
10. The Bohr effect is that hemoglobin’s oxygen affinity ______________ as the pH _________________.
11. Two compounds, ____________ and _____________ help hemoglobin to form salt bridges that stabilize the (R orT?)-state and therefore decrease oxygen binding affinity. This causes (more or less?) oxygen to be released.
12. What particular mutation leads to sickle-cell anemia? How does this mutation cause the disease?