Abstract
For many years, hemoglobin (Hb) has been a model protein for studies of factors that affect the conformational states of proteins1. Natural Hb variants and recombinant Hbs that possess single amino acid residue substitutions have provided important information on the contributions of specific sites to interactions at the interface between the dimer pairs involved in the allosteric transition as the Hb tetramer moves between its oxy and deoxy conformations2. The recent unexpected finding3 that the interactions between these dimer pairs are much stronger in fetal Hb [HbF; (αγ)2] than in adult Hb [HbA; (αβ)2; see Fig. 1) has opened new avenues for exploration of sequence– function relationships in proteins.
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