Model-potential-free analysis of small angle scattering of proteins in solution: insights into solvent effects on protein-protein interaction

Phys Chem Chem Phys. 2014 Dec 14;16(46):25492-7. doi: 10.1039/c4cp03606a. Epub 2014 Oct 24.

Abstract

To extract protein-protein interaction from experimental small-angle scattering of proteins in solutions using liquid state theory, a model potential consisting of a hard-sphere repulsive potential and the excess interaction potential has been introduced. In the present study, we propose a model-potential-free integral equation method that extracts the excess interaction potential by using the experimental small-angle scattering data without specific model potential such as the Derjaguin-Landau-Verwey-Overbeek (DLVO)-type model. Our analysis of experimental small-angle X-ray scattering data for lysozyme solution shows both the stabilization of contact configurations of protein molecules and a large activation barrier against the formation of the contact configurations in addition to the screened Coulomb repulsion. These characteristic features, which are not well-described by the DLVO-type model, are interpreted as solvent effects.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Models, Molecular*
  • Muramidase / chemistry*
  • Muramidase / metabolism*
  • Protein Binding / drug effects
  • Scattering, Small Angle*
  • Solutions
  • Solvents / pharmacology*
  • X-Ray Diffraction

Substances

  • Solutions
  • Solvents
  • Muramidase