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Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution.

Maria Grazia Ortore1, Francesco Spinozzi, Paolo Mariani

  • 1Dipartimento SAIFET, Sezione Scienze Fisiche, Università Politecnica delle Marche and CNISM, Ancona, Italy. mg.ortore@alisf1.univpm.it; russo@ill.fr

Journal of the Royal Society, Interface
|July 3, 2009
PubMed
Summary

High pressure alters lysozyme interactions and dynamics in solution. Changes in protein-protein interactions and hydration water structure occur around 600-1000 bar, affecting protein mobility.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Understanding protein behavior under pressure is crucial for various biological and industrial applications.
  • Lysozyme is a model protein extensively studied for its structural and functional properties.

Purpose of the Study:

  • To investigate high-pressure-induced changes in lysozyme's structure, protein-protein interactions, and dynamics in solution.
  • To elucidate the role of hydration water in pressure-induced modifications.

Main Methods:

  • Small-angle X-ray scattering (SAXS) to determine low-resolution structure and interactions.
  • Elastic and quasi-elastic neutron scattering to probe protein and hydration water dynamics.
  • Advanced data analysis including global-fit procedures for hydrated protein form factor description.

Main Results:

  • Lysozyme maintains its globular structure up to 1500 bar.
  • Significant changes in protein-protein interaction potential observed between 600-1000 bar.
  • Discontinuity in hydration water mass density and evolution of protein dynamics (diffusing to localized motions) within the same pressure range.

Conclusions:

  • High pressure significantly modifies protein-protein interactions and hydration water properties in lysozyme solutions.
  • Pressure-induced changes in the first hydration layer's water configuration are proposed to drive alterations in local protein mobility.
  • SAXS and neutron scattering provide complementary insights into pressure effects on protein structure and dynamics.