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Mapping Hydration Dynamics around a β-Barrel Protein.

Jin Yang1, Yafang Wang1, Lijuan Wang1

  • 1Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.

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This summary is machine-generated.

Protein hydration dynamics are heterogeneous around both alpha-helical and beta-sheet proteins. Hydration water dynamics are faster than protein relaxations, influencing protein fluctuations and differing between secondary structures.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Protein surface hydration is crucial for protein structure, flexibility, dynamics, and function.
  • Understanding the relationship between protein structure and hydration dynamics is challenging.

Purpose of the Study:

  • To systematically characterize hydration dynamics around a beta-barrel protein, rat liver fatty acid-binding protein (rLFABP).
  • To reveal the effect of different protein secondary structures (beta-sheet vs. alpha-helical) on hydration water behavior.

Main Methods:

  • Employed a tryptophan scan on the protein surface, examining 17 different sites.
  • Utilized ultrafast spectroscopy to observe hydration water relaxation and tryptophan side chain anisotropy dynamics.

Main Results:

  • Observed three distinct hydration water relaxation time scales (hundreds of femtoseconds to hundreds of picoseconds).
  • Identified two distinct tryptophan side chain relaxation time scales (tens to hundreds of picoseconds).
  • Found hydration dynamics are heterogeneous, with outer-layer water relaxing faster (hundreds of femtoseconds) and inner-layer water relaxing on picosecond to hundred-picosecond time scales.

Conclusions:

  • Hydration dynamics are faster than protein relaxations and drive picosecond-scale protein fluctuations.
  • Hydration dynamics are generally slower around beta-sheet structures compared to alpha-helical motifs.
  • Beta-sheet proteins exhibit thicker hydration shells and more rigid interfacial hydration networks than alpha-helical proteins.