van Oss C J, Good R J
Department of Microbiology, State University of New York, Buffalo 14214.
J Protein Chem. 1988 Apr;7(2):179-83. doi: 10.1007/BF01025248.
Through contact-angle measurements with a number of liquids, on layers of hydrated human serum albumin (HSA), built on anisotropic ultrafilter membranes, the apolar, Lifshitz-van der Waals surface tension component, as well as the polar, electron-acceptor and electron-donor parameters of the hydrated layers could be determined. From these data, it was found that the degree of orientation of the water molecules of hydration of HSA is approximately 98% in the first layer of hydration and approximately 30% of the second layer. The water molecules of hydration are oriented with the H atoms closest to, and the O atoms farthest from, the protein surface.
通过对多种液体与构建在各向异性超滤膜上的水合人血清白蛋白（HSA）层进行接触角测量，可以确定水合层的非极性、Lifshitz-范德华表面张力分量以及极性、电子受体和电子供体参数。从这些数据发现，HSA水合水分子的取向程度在第一层水合中约为98%，在第二层中约为30%。水合水分子的取向是H原子最靠近蛋白质表面，而O原子离蛋白质表面最远。
