Question: In hemoglobin Rainier, Tyr 145 is replaced by Cys, which forms a disulfide bond with another Cys residue in the same subunit. This prevents the
In hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cys residue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to
(a) Oxygen affinity,
(b) The Bohr effect, and
(c) The Hill constant?
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a Because the mutation destabilizes the T conformation of hemoglobin ... View full answer
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