1. Summarize how oxygen binds to hemoglobin.
2. Outline how oxygen binding brings about conformation change in hemoglobin.
3. Compare deoxyhemoglobin and oxyhemoglobin conformations.
4. Explain the origin of higher oxygen affinity of hemoglobin’s R conformation.
5. Compare and contrast the MWC and KNF models of protein conformation change.
6. Contrast “conformation selection” vs. “induced fit” allostery.
7. Illustrate how allosteric effectors/modulators work.
