Nonlinear pressure dependence of the interaction potential of dense protein solutions

Phys Rev Lett. 2011 Apr 29;106(17):178102. doi: 10.1103/PhysRevLett.106.178102. Epub 2011 Apr 26.

Abstract

The influence of pressure on the structure and protein-protein interaction potential of dense protein solutions was studied and analyzed using small-angle x-ray scattering in combination with a liquid state theoretical approach. The structural as well as the interaction parameters of dense lysozyme solutions are affected by pressure in a nonlinear way. The structural properties of water lead to a modification of the protein-protein interactions below 4 kbar, which might have significant consequences for the stability of proteins in extreme natural environments.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrogen-Ion Concentration
  • Models, Chemical
  • Muramidase / chemistry*
  • Muramidase / metabolism
  • Nonlinear Dynamics
  • Pressure
  • Protein Folding
  • Protein Structure, Secondary
  • Scattering, Radiation
  • Solutions / chemistry*
  • X-Rays

Substances

  • Solutions
  • Muramidase