The influence of weakly polar solvent chloroform on the state of water adsorbed by serum albumin

Abstract

The hydration shell structure of human serum albumin (HSA) and HSA adsorbed on a surface of highly disperse silica in a weakly polar solvent (chloroform) or with various addition of this solvent was studied by 1 H NMR spectroscopy and 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 levels and filled up with structured water unfrozen at T < 273.