Hi, I have a question about the binding of BPG on wild-type hemoglobin. Lys82, w

Question

Hi, I have a question about the binding of BPG on wild-type hemoglobin. Lys82, which stabilizes the R-state, would be present, but our teacher mentioned that Lys82 can start opposing the T-state before it binds to BPG. BPG can’t do anything until it binds to hemoglobin, however, so would BPG not be able to reduce oxygen affinity since with the lysine already there it would be in the R state?? Hi, I have a question about the binding of BPG on wild-type hemoglobin. Lys82, which stabilizes the R-state, would be present, but our teacher mentioned that Lys82 can start opposing the T-state before it binds to BPG. BPG can’t do anything until it binds to hemoglobin, however, so would BPG not be able to reduce oxygen affinity since with the lysine already there it would be in the R state??

Explanation / Answer

Answer: BPG binding is necessary to reduce the oxygen affinity. Since T state has only one binding site for BPG but, none for R state. It is due to conformational change of haemoglobin structure at Lys82.

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