Abstract
HAEMOGLOBIN is a tetramer (two α and two β subunits) in natural conditions in erythrocytes. I have studied the relationship between quaternary structure and haemoglobin function to determine the sequence of molecular events within the tetramer that bring about the conformational change (from constrained to unconstrained structures1,2) responsible for cooperative ligand binding3. In most technically accessible conditions, however, the tetramer exists in a dissociation-association equilibrium with dimer4–10. To elucidate the tetramer mechanism, therefore, it had to be determined whether the free dimer may undergo an equivalent conformational transition; that is, whether the dimer possesses the functional interactions responsible for cooperativity in the tetramer11–13.
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KELLETT, G. Ligand-free Haemoglobin Dimers. Nature New Biology 234, 189–191 (1971). https://doi.org/10.1038/newbio234189a0
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DOI: https://doi.org/10.1038/newbio234189a0
