Changes in serum albumin hydration at thermoinduced structural transitions in solutions differing in viscosity.

Abstract

The hydration of human serum albumin in solutions differing in viscosity has been studied in the temperature range of 10-40 degrees C in order to determine the nature of changes in protein hydration at thermoinduced structural transitions. The NMR technique was employed to determine the effective number of protein-bound water molecules (n) considered as a… (More)

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