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

Yangzhong Qin, Yi Yang, Lijuan Wang, Dongping Zhong

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)658-665
Number of pages8
JournalChemical Physics Letters
Volume683
DOIs
Publication statusPublished - 2017 Sep 1

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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