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Spatially Heterogeneous Surface Water Diffusivity around Structured Protein Surfaces at Equilibrium.

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Hydration water dynamics vary across protein surfaces, with hydrophobic regions showing slower water diffusion. This heterogeneity suggests proteins encode information in their hydration shells.

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Structural Biology

Background:

  • Hydration water is crucial for protein-ligand interactions.
  • Understanding water's role requires probing its dynamics on protein surfaces.
  • Local variations in water properties are key to protein function.

Purpose of the Study:

  • To investigate site-specific hydration water dynamics on a protein surface.
  • To correlate water dynamics with local protein surface properties.
  • To compare water dynamics across different biomolecular surfaces.

Main Methods:

  • Overhauser dynamic nuclear polarization (ODNP) to probe water dynamics.
  • Molecular dynamics (MD) simulations to determine protein surface hydropathy.
  • Site-specific labeling for targeted measurements.

Main Results:

  • Hydration water dynamics (diffusive water) are heterogeneous across the Chemotaxis Y (CheY) protein surface.
  • Slower water diffusion correlates with more hydrophobic protein surface sites.
  • Globular proteins exhibit more heterogeneous water dynamics than IDPs, peptides, and liposomes.

Conclusions:

  • Protein surface structure dictates local hydration water dynamics.
  • Structured proteins can encode information within their hydration shells.
  • Hydration water heterogeneity is a fundamental aspect of protein biophysics.