Mapping hydration dynamics around a protein surface

Luyuan Zhang, Lijuan Wang, Ya-Ting Kao, Weihong Qiu, Yi Yang, Oghaghare Okobiah, Dongping Zhong*

*Corresponding author for this work

Research output: Contribution to journalArticle

236 Scopus citations

Abstract

Protein surface hydration is fundamental to its structure and activity. We report here the direct mapping of global hydration dynamics around a protein in its native and molten globular states, using a tryptophan scan by site-specific mutations. With 16 tryptophan mutants and in 29 different positions and states, we observed two robust, distinct water dynamics in the hydration layer on a few (≈1-8 ps) and tens to hundreds of picoseconds (≈20-200 ps), representing the initial local relaxation and subsequent collective network restructuring, respectively. Both time scales are strongly correlated with protein's structural and chemical properties. These results reveal the intimate relationship between hydration dynamics and protein fluctuations and such biologically relevant water-protein interactions fluctuate on picosecond time scales.

Original languageEnglish
Pages (from-to)18461-18466
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume104
Issue number47
DOIs
StatePublished - 20 Nov 2007

Keywords

  • Femtosecond dynamics
  • Site-directed mutation
  • Tryptophan scan
  • Water-protein fluctuation

Fingerprint Dive into the research topics of 'Mapping hydration dynamics around a protein surface'. Together they form a unique fingerprint.

  • Cite this