2013 Fiscal Year Final Research Report
Study on the hydration structural changes in coupling with the internal motions of proteins using time-resolved fluorscence measurement
| Project/Area Number |
22244054
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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 |
Biophysics/Chemical physics
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| Research Institution | Keio University |
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Principal Investigator |
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| Project Period (FY) |
2010-04-01 – 2014-03-31
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| Keywords | タンパク質水和 / 水和構造 / 分子動力学シミュレーション / 蛍光分光 / 和周波測定 / 非線形光学 / Ｘ線結晶構造解析 / 主成分分析 |
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| Research Abstract |
Proteins are engaged in the elementary processes of life in cells and fold and function only in aqueous environment. To understand why water is indispensable for proteins it is necessary to visualize the hydration structures of proteins at spatial resolution of atomic level and ps temporal resolution. In this research project, through developing time-resolved fluorescence measurement system dedicated for proteins, we analyzed the dynamics of protein hydration from the experimental point of view using the fluorescence measurement and structure analyses as well as molecular dynamics simulation.
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[Journal Article] Light-induced conformational changes of LOV (Light Oxygen Voltage-sensing domain) 1 and LOV2 relative to the kinase domain and regulation of kinase activity in Chlamydomonas phototropin2014
Author(s)
K. Okajima, Y. Aihara, Y. Takayama, M. Nakajima, S. Kashojiya, T. Hikima, T. Oroguchi, A. Kobayashi, Y. Sekiguchi, M. Yamamoto, T. Suzuki, A. Nagatani, M. Nakasako and S. Tokutomi
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Journal Title
Journal of Biological Chemistry
Volume: 289
Pages: 413-422
DOI
Peer Reviewed
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