MEASUREMENT OF LIGAND-INDUCED CONFORMATIONAL CHANGES IN HEMOGLOBIN BY CIRCULAR DICHROISM
- 1 May 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 63 (1), 205-212
- https://doi.org/10.1073/pnas.63.1.205
Abstract
The UV circular-dichroism spectra of human and horse hemoglobins have been determined at various degrees of partial saturation with oxygen. Spectra of the two native hemoglobins were compared with spectra of the corresponding proteins modified with a reagent known to eliminate the conformational rearrangement normally associated with cooperativity. Such comparison indicates that one region, around 260 mmu, is sensitive chiefly to the state of the hemes; changes in another region, around 285 mmu, may be correlated with the conformational transformation linked to cooperative interactions. All circular-dichroism changes are strictly linear with fractional saturation with oxygen. Possible implications of these results to recently proposed mechanisms for cooperativity in proteins are discussed.Keywords
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