Biopolymers and cell. 2006; 22 (5): 375 - 383

The Influence of Weakly Polar Solvent Chloroform on the State of Water Adsorbed by Serum Albumin

O.V. Nechypor, V.M. Gun’ko, V.M. Barvinchenko, V.V. Turov

The hydrate shell structure of dry human serum albumin and albumin adsorbed on a surface of highly disperse silica in a weakly polar solvent (chloroform) or with addition of this solvent was studied by ¹H NMR spectroscopy with layer-by-layer freezing out of a liquid phase. The influence of chloroform can result in changes in the ratio of volumes of internal regions of protein globule characterized by different hydration level and filled up with structured water unfrozen at T < 273º.

Key words: human serum albumin, highly disperse silica, chloroform, ¹H NMR spectroscopy.