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How proteins modify water dynamics.

Filip Persson1, Pär Söderhjelm1, Bertil Halle1

  • 1Division of Biophysical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden.

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Summary
This summary is machine-generated.

Protein surface topography, not polarity, dictates hydration water dynamics. Water rotation transitions from collective to exchange-mediated randomization (EMOR) with increasing confinement, explaining the rotational perturbation factor (RPF).

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Computational Biology

Background:

  • Protein-water interactions are crucial for biological processes.
  • 17O magnetic relaxation dispersion (MRD) probes hydration layer dynamics.
  • Previous studies show hydration water rotation is 3-5x slower than bulk water.

Purpose of the Study:

  • Resolve the role of protein surface polarity versus topography in hydration water dynamics.
  • Investigate the molecular mechanisms governing water rotational correlation times (TCFs).
  • Compare simulated and experimental 17O MRD profiles.

Main Methods:

  • Analysis of extensive molecular dynamics simulations for four globular proteins and three water models.
  • Calculation of rotational time correlation functions (TCFs) and rotational perturbation factors (RPFs).
  • Computation of full 17O MRD profiles, including low-frequency dispersion.

Main Results:

  • Protein-water interaction dynamics are primarily determined by surface topography (confinement), not polarity.
  • Water rotation interpolates between collective and exchange-mediated orientational randomization (EMOR) mechanisms.
  • A 30% discrepancy between simulated and measured RPFs suggests force field imperfections.

Conclusions:

  • Hydration water dynamics are governed by a confinement index, with polarity being a secondary effect.
  • The EMOR mechanism significantly contributes to the observed RPF, previously unrecognized in simulations.
  • 17O TCF is highly sensitive to short-range protein-water interactions.