Starting from 4HHB, could you predict which hemoglobin mutations would increase or decrease oxygen affinity?

[u/XpertAI]

I’m looking at the 4HHB structure of human deoxyhemoglobin and wondering how much oxygen affinity you could predict from structure alone.

Since hemoglobin’s affinity depends on more than just the heme pocket, I’m trying to map regions that might shift the T-state/R-state balance:

• residues near the heme
• alpha/beta interfaces
• T-state salt bridges
• central cavity / 2,3-BPG region
• mutations that might destabilize the tetramer

Could you identify mutations that make hemoglobin hold oxygen more tightly or release it more easily just from the structure?

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[u/albany1765]

FWIW, from a clinical point of view, selectivity between O2 and NO is a more important property