Amino acid substitutions at the interfaces of the a and B subunits of hemoglobin can change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost. As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as a ligand. Explain.

Human Physiology: From Cells to Systems (MindTap Course List)
9th Edition
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Lauralee Sherwood
Chapter11: The Blood
Section: Chapter Questions
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Amino acid substitutions at the interfaces of the a and B subunits of hemoglobin can
change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant
hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost.
As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as
a ligand. Explain.
Transcribed Image Text:Amino acid substitutions at the interfaces of the a and B subunits of hemoglobin can change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost. As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as a ligand. Explain.
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