Abstract
The deuterium and the proton spin–spin relaxation times are investigated at 4 MHz in partially deuterated samples of hemoglobin A and S at 36 °C during spontaneous deoxygenation. Deuterium relaxation shows a sigmoidal behavior describing the three characteristic phases of hemoglobin S (HbS) polymerization. The coincidence between the behaviors of deuterium and proton relaxation supports the dominant effect of agglutination on macromolecular mobility. Evidences of an increase of the internal electric field gradient and the appearance of a modified charge distribution inside the HbS solution, as a result of the polymerization process under spontaneous deoxygenation, were not found.
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