2017 Fiscal Year Final Research Report
Investigation on the dynamics of protein folding by single molecule fluorescence spectroscopy
| Project Area | Science on Function of Soft Molecular Systems by Cooperation of Theory and Experiment |
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| Project/Area Number |
25104007
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| Research Category |
Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
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| Allocation Type | Single-year Grants |
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| Review Section |
Science and Engineering
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| Research Institution | Tohoku University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
KAMAGATA Kiyoto 東北大学, 多元物質科学研究所, 助教 (90432492)
OIKAWA Hiroyuki 東北大学, 多元物質科学研究所, 助教 (40536778)
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| Research Collaborator |
MANO Eriko 東北大学, 多元物質科学研究所, 技術補佐員
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| Project Period (FY) |
2013-06-28 – 2018-03-31
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| Keywords | タンパク質ダイナミクス / フォールディング / 一分子蛍光分光法 / p53 |
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| Outline of Final Research Achievements |
We developed a new method of single molecule fluorescence detection that can track single-molecule fluorescence and FRET efficiency at the time resolution of 10 microsecond. We used the method for the investigation of the folding dynamics of proteins, and revealed the unexpected heterogeneity in the unfolded state of BdpA and ubiquitin. In addition, we constructed a fluorescence microscope that can image the sliding of a tumor suppressor p53 along the stretched DNA, and revealed its target search dynamics. We clarified various properties of p53 including the dependency of the target search on the divalent cations, the behavior of p53 near the target sequence and the roles of disordered linker in p53. The current results might open a new research field of investigating proteins based on the assimilation of data obtained by single molecule method and MD calculation. In addition, investigations of the dynamics of proteins in the environment mimicking nucleus might become possible.
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| Free Research Field |
生物物理学、物理化学、タンパク質科学
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