Orientation of the water molecules of hydration of human serum albumin.
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.
van Oss
C J
CJ
Department of Microbiology, State University of New York, Buffalo 14214.
Good
R J
RJ
D006801:Humans; D006860:Hydrogen Bonding; D012709:Serum Albumin; D012995:Solubility; D013500:Surface Tension; D014462:Ultrafiltration; D014867:Water
D012709:Serum Albumin; D014867:Water