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Model-potential-free analysis of small angle scattering of proteins in solution: insights into solvent effects on protein–protein interaction
Author(s) -
Tomonari Sumi,
Hiroshi Imamura,
Takeshi Morita,
Yasuhiro Isogai,
Keiko Nishikawa
Publication year - 2014
Publication title -
physical chemistry chemical physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.053
H-Index - 239
eISSN - 1463-9084
pISSN - 1463-9076
DOI - 10.1039/c4cp03606a
Subject(s) - scattering , protein–protein interaction , small angle scattering , chemistry , protein structure , chemical physics , computational chemistry , physics , biochemistry , optics
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.

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