Article
Protein surface hydration mapped by site-specific mutations.
Proceedings of the National Academy of Sciences of the United States of America - 19 Sept 2006
Qiu Weihong, Kao Ya-Ting, Zhang Luyuan, Yang Yi, Wang Lijuan, Stites Wesley E, Zhong Dongping, Zewail Ahmed H
Abstract excerpt
Water motion at protein surfaces is fundamental to protein structure, stability, dynamics, and function. By using intrinsic tryptophans as local optical probes, and with femtosecond resolution, it is possible to probe surface-water motions in the hydration layer. Here, we report our studies of local hydration dynamics at the surface of the enzyme Staphylococcus nuclease using site-specific mutations. From these...
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