Abstract
Summary Iodoacetamide spin-labels bound to the F9(93)β cysteine residues of hemoglobin S are sensitive to changes in environment induced by a decrease in temperature or an increase in viscosity, yet show no change in ESR spectrum upon aggregation (gelation) of the deoxyhemoglobin. Similar results are found with two different spin-labels having different chain lengths between the nitroxide radical and the cysteine residue. The fact that the environment which the F9(93)β cysteine residues experience in the gel is indistinguishable from that experienced in solution indicates that they are not located in close proximity to any of the sites of interaction between individual deoxyhemoglobin S tetramers and that while the viscosity of a deoxyhemoglobin S solution changes enormously upon gelation, the microviscosity within the gel can not be greatly changed.
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