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ID 57459
フルテキストURL
著者
Sumi, Tomonari Department of Chemistry, Faculty of Science, Okayama University ORCID Kaken ID publons researchmap
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
抄録
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.
発行日
2014-10-17
出版物タイトル
Physical Chemistry Chemical Physics
16巻
46号
出版者
Royal Society of Chemistry
開始ページ
25492
終了ページ
25497
ISSN
14639076
NCID
AA11301773
資料タイプ
学術雑誌論文
言語
English
OAI-PMH Set
岡山大学
論文のバージョン
author
PubMed ID
DOI
Web of Science KeyUT
関連URL
isVersionOf https://doi.org/10.1039/c4cp03606a
Citation
Phys. Chem. Chem. Phys., 2014,16, 25492-25497
助成機関名
文部科学省
助成番号
25610121 : Chemomechanical network modeling for molecular motor dynamics of kinesin