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. 1969 May;63(1):205–212. doi: 10.1073/pnas.63.1.205

MEASUREMENT OF LIGAND-INDUCED CONFORMATIONAL CHANGES IN HEMOGLOBIN BY CIRCULAR DICHROISM

Sanford R Simon 1,2, Charles R Cantor 1,2
PMCID: PMC534023  PMID: 5257964

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 mμ, is sensitive chiefly to the state of the hemes; changes in another region, around 285 mμ, 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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