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ID 57459
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Author
Sumi, Tomonari Department of Chemistry, Faculty of Science, Okayama University ORCID Kakenhi
Imamura, Hiroshi Graduate School of Advanced Integration Science, Chiba University
Morita, Takeshi Graduate School of Advanced Integration Science, Chiba University
Isogai, Yasuhiro Department of Biotechnology, Toyama Prefectural University
Nishikawa, Keiko Graduate School of Advanced Integration Science, Chiba University
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.
Published Date
2014-10-17
Publication Title
Physical Chemistry Chemical Physics
Volume
volume16
Issue
issue46
Publisher
Royal Society of Chemistry
Start Page
25492
End Page
25497
ISSN
14639076
NCID
AA11301773
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
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author
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DOI
Web of Sience KeyUT
Related Url
isVersionOf https://doi.org/10.1039/c4cp03606a
Citation
Phys. Chem. Chem. Phys., 2014,16, 25492-25497
Funder Name
Ministry of Education, Culture, Sports, Science and Technology
助成番号
25610121 : Chemomechanical network modeling for molecular motor dynamics of kinesin