Abstract
The mechanism of denaturation of human serum albumin (HSA) under action of a cationic detergent—cethyltrimethylammonium bromide (CTAB) is investigated by Raman spectroscopy method. The percentage contents of α-helical segments in polypeptide chain of HSA at denaturation under action of different concentrations of CTAB at different values of pH is determined. It is shown, that more intensive denaturation of HSA under action of CTAB takes place at pH values, larger the isoelectric point of protein (pI 4.7).
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