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MAPPING HYDRATION DYNAMICS AND COUPLED WATER-PROTEIN FLUCTUATIONS AROUND A PROTEIN SURFACE

Please use this identifier to cite or link to this item: http://hdl.handle.net/1811/33266

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Title: MAPPING HYDRATION DYNAMICS AND COUPLED WATER-PROTEIN FLUCTUATIONS AROUND A PROTEIN SURFACE
Creators: Zhang, Luyuan; Wang, Lijuan; Kao, Ya-Ting; Qiu, Weihong; Yang, Yi; Okobiah, Oghaghare; Zhong, Dongping
Issue Date: 2008
Abstract: Elucidation of the molecular mechanism of water-protein interactions is critical to understanding many fundamental aspects of protein science, such as protein folding and misfolding and enzyme catalysis. We recently carried out a global mapping of protein-surface hydration dynamics around a globular $\alpha$-helical protein apomyoglobin. The intrinsic optical probe tryptophan was employed to scan the protein surface one at a time by site-specific mutagenesis. With femtosecond resolution, we mapped out the dynamics of water-protein interactions with more than 20 mutants and for two states, native and molten globular. A robust bimodal distribution of time scales was observed, representing two types of water motions: local relaxation and protein-coupled fluctuations. The time scales show a strong correlation with the local protein structural rigidity and chemical identity. We also resolved two distinct contributions to the overall Stokes-shifts from the two time scales. These results are significant to understanding the role of hydration water on protein structural stability, dynamics and function.
URI: http://hdl.handle.net/1811/33266
Other Identifiers: 2008-WJ-03
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