Measurement of Ligand-induced Conformational Changes in Hemoglobin by Circular Dichroism
Year: 1969
Type: article
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.
Authors: Sanford R. Simon, Charles R. Cantor
Institutions: Columbia University, Rockefeller University
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2127598700