ID | 57459 |
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Author |
Sumi, Tomonari
Department of Chemistry, Faculty of Science, Okayama University
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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
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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.
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Published Date | 2014-10-17
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Publication Title |
Physical Chemistry Chemical Physics
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Volume | volume16
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Issue | issue46
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Publisher | Royal Society of Chemistry
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Start Page | 25492
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End Page | 25497
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ISSN | 14639076
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NCID | AA11301773
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Content Type |
Journal Article
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language |
English
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OAI-PMH Set |
岡山大学
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File Version | author
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Related Url | isVersionOf https://doi.org/10.1039/c4cp03606a
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Citation | Phys. Chem. Chem. Phys., 2014,16, 25492-25497
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Funder Name |
Ministry of Education, Culture, Sports, Science and Technology
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助成番号 | 25610121 : Chemomechanical network modeling for molecular motor dynamics of kinesin
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