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In one of the beta chains of normal adult Hemoglobin structure, H146 ends up in close proximity to D94 on the same chain when oxygen is delivered to the tissues. Hypothetically, one of the H146 on the beta chain has been changed to a D through mutation. What effect, if any does this mutation have on oxygen binding by the mutated hemoglobin, compared to normal hemoglobin? What effect, if any does this mutation have on the Bohr Effect of the mutant hemoglobin?

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