2017 Fiscal Year Final Research Report
All-Atom Analysis of Cosolvent Effect on Protein Structure through Free-Energy Calculation
| Project/Area Number |
26240045
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Life / Health / Medical informatics
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| Research Institution | Osaka University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
三本木 至宏 広島大学, 生物圏科学研究科, 教授 (10222027)
石塚 良介 大阪大学, 基礎工学研究科, 助教 (30462196)
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| Project Period (FY) |
2014-04-01 – 2018-03-31
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| Keywords | 溶媒和 / 共溶媒 / 構造ゆらぎ / 変性 / 分布関数理論 / 分子シミュレーション / 分子間相互作用 / 水 |
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| Outline of Final Research Achievements |
Energetics of protein was analyzed in pure-water solvent and in a set of mixed solvents with urea and its alkylated derivatives. The solvation free energy was computed through all-atom molecular dynamics simulation combined with the solution theory in the energy representation, and its correlations were examined against the electrostatic and van der Waals components in the the protein-solvent interaction and the excluded-volume component. It was observed in pure-water solvent that the solvation free energy varies in parallel to the electrostatic component with minor roles played by the other components. The effect of urea or its alkylated derivative on protein structure was investigated in terms of the free-energy change upon transfer of the protein solute from pure-water solvent to the mixed solvent, and it was found from the correlations of the transfer free energy to the interaction components that the denaturing effect of the cosolvent is due to the van der Waals interaction.
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| Free Research Field |
物理化学、理論化学、溶液化学、生物物理学
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