Theoretical Study of Molecular functions of Proteins
Project/Area Number |
16H04776
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Kyoto University |
Principal Investigator |
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Project Period (FY) |
2016-04-01 – 2019-03-31
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Project Status |
Completed (Fiscal Year 2018)
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Budget Amount *help |
¥17,420,000 (Direct Cost: ¥13,400,000、Indirect Cost: ¥4,020,000)
Fiscal Year 2018: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2017: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2016: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
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Keywords | 分子シミュレーション / 光受容体タンパク質 / 酵素反応 / 光遺伝学 / QM/MM 法 / 分子モーター / 光受容体 |
Outline of Final Research Achievements |
Protein functions are fulfilled by correlation among various phenomena on different spatial and temporal scales ranging from enzymatic reactions to global conformational changes of proteins. By using a novel molecular simulation approach developed recently by us, QM/MM RWFE-SCF, which is capable of describing such correlations of various phenomena on different scale, we succeeded in obtaining novel molecular mechanistic insights into photo-activation processes of LOV photo-receptor and channelrhodopsin, and enzymatic catalysis of HIV protease.
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Academic Significance and Societal Importance of the Research Achievements |
本研究で扱っている光受容体タンパク質や酵素では、その顕著な分子機能において、光化学反応や酵素反応などの局所的な電子状態変化と大きなタンパク質分子の構造変化のスケールの異なる現象が関わっており、従来の理論的解析が困難であった。本研究では、新規の理論的手法により、その困難を解決し、原子レベルからの分子機構の解明に成功した。これにより、神経科学分野における新規なタンパク質ツールの開発や、 HIV 感染の治療薬における薬剤耐性の問題の解決に向けての道が開かれた。
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Report
(4 results)
Research Products
(22 results)
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[Journal Article] X-ray crystallographic structure of thermophilic rhodopsin: implications for high thermal stability and optogenetic function2016
Author(s)
Tsukamoto T, Mizutani K, Hasegawa T, Takahashi M, Honda N, Hashimoto N, Shimono K, Yamashita K, Yamamoto M, Miyauchi S, Takagi S, Hayashi S, Murata T, Sudo Y.
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Journal Title
J. Biol. Chem.
Volume: in press
Issue: 23
Pages: 12223-12232
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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