Abstract
Using variable temperature techniques, the spin label spectral resolution of hemoglobin labeled at the β93 cysteines with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)iodoacetamide has been greatly enhanced. The effects of different ligands, inositol hexaphosphate, pH and salt concentration upon spin labeled ferrous and ferric hemoglobin indicate that the β chain tertiary structure exhibits considerable variability within the oxy and deoxy quaternary structures. From these studies ligand and spin state changes both appear to be of significance in producing structural changes; binding of inositol hexaphosphate then produces further structural changes secondary in amplitude.
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