BIOCH200 Lecture Notes - Lecture 15: Supreme Headquarters Allied Powers Europe, Myoglobin, Bohr Effect
15 Oct 2016
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Biochem 200 - lecture #15 - protein function pt. Myoglobin and hemoglobin: similar functions: reversibly bind and release oxygen, different functions. Hb: oxygen transport from lungs to tissues. Difference in ppo2: sigmoidal oxygen binding curve. How does hb change its affinity for o2: there are 2 distinct structures of hemoglobin. The subunit interface changes: tense (t) state. Similar to myoglobin in terms of oxygen binding site. The difference between the two states aren"t huge, but the size of oxygen is small enough that it has a significant affect on the two states. Contact between subunits: basically his is important, because it changes spots when it goes from t to r state, conformational change in hb structure. Less internal space in r state (less interface contact) and vice versa for t: his is also important for myoglobin and hemoglobin. Summarization: equilibrium between r and t. Oxygen influences equilibrium by shifting to the oxy bound state (r)
