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Protein hydration in aqueous solution.

G Otting1, E Liepinsh, K Wüthrich

  • 1Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.

Science (New York, N.Y.)
|November 15, 1991
PubMed
Summary

High-resolution nuclear magnetic resonance (NMR) studies reveal two distinct protein hydration sites in aqueous solution. Interior protein water molecules exhibit longer residence times compared to surface-adsorbed water molecules.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Understanding protein hydration is crucial for biological processes.
  • Previous studies using X-ray crystallography provided insights into ordered water molecules in protein crystals.
  • The dynamic behavior of protein-bound water in solution remained less understood.

Purpose of the Study:

  • To investigate the distinct types of protein hydration sites in aqueous solution.
  • To characterize the residence times and dynamics of water molecules interacting with proteins.
  • To differentiate between interior and surface hydration water behavior.

Main Methods:

  • High-resolution proton nuclear magnetic resonance (NMR) spectroscopy.
  • Analysis of protein hydration in aqueous solutions.
  • Measurement of water molecule residence times.

Main Results:

  • Identified two qualitatively different types of protein hydration sites.
  • Observed a small population of interior protein water molecules with residence times from 10^-2 to 10^-8 seconds.
  • Characterized surface hydration water molecules with subnanosecond residence times, even in sites with ordered water in crystal structures.

Conclusions:

  • Protein hydration is heterogeneous, with distinct interior and surface water populations.
  • Interior protein-bound water exhibits significantly longer residence times than surface-bound water.
  • NMR spectroscopy is a powerful tool for elucidating the dynamics of protein hydration in solution.

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