Abstract
Abstract: The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β (C93A+C 112G), have been determined at 2.0 A and 1.8 A resolution, respectively. Oxygen molecules fully occupy the, α -heme and partially occupy the a.,-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.
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