Wednesday, March 15, 2017

Abstract-Dynamics of hydration water and coupled protein sidechains around a polymerase protein surface

  • Department of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, OH 43210

Water-protein coupled interactions are essential to the protein structural stability, flexibility and dynamic functions. The ultimate effects of the hydration dynamics on the protein fluctuations remain substantially unexplored. Here, we investigated the dynamics of both hydration water and protein sidechains at 13 different sites around the polymerase β protein surface using a tryptophan scan with femtosecond spectroscopy. Three types of hydration-water relaxations and two types of protein sidechain motions were determined, reflecting a highly dynamic water-protein interactions fluctuating on the picosecond time scales. The hydration-water dynamics dominate the coupled interactions with higher flexibility.

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