Issue 46, 2014

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

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.

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

Supplementary files

Article information

Article type
Paper
Submitted
13 Aug 2014
Accepted
17 Oct 2014
First published
17 Oct 2014

Phys. Chem. Chem. Phys., 2014,16, 25492-25497

Author version available

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

T. Sumi, H. Imamura, T. Morita, Y. Isogai and K. Nishikawa, Phys. Chem. Chem. Phys., 2014, 16, 25492 DOI: 10.1039/C4CP03606A

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