Abstract
Nuclear magnetic resonance spectra of Hb A and Hb Chesapeake in both carboxy- and deoxy-forms suggest that (1) there are differences in the aromatic proton resonances between these two proteins which may be due to the altered interactions among the amino acid residues at α 1-β 2 contacts as a result of the amino acid substitution at α-92 in Hb Chesapeake, and (2) amino acid residues at FG3 (leucine) and/or FG5 (valine) may be responsible for transmitting information from α 1 to β 2 chain or vice versa in the course of oxygenation of hemoglobin.
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