Abstract
Structural changes in human serum albumin (HSA) induced by low temperatures in water-dimethyl sulfoxide (DMSO) solutions were studied by fluorescent spectroscopy. The emission, synchronous, and isopotential synchronous spectra (3D spectra) of the HSA were analyzed. It was shown that protein does not undergo drastic structural changes in the fast freezing/defrosting mode in solutions of up to 20% DMSO but becomes more compact.
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