Unified understanding of the coupled folding and binding mechanisms of intrinsically disordered proteins
| Project/Area Number |
15K07023
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | The University of Tokyo |
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Principal Investigator |
Arai Munehito 東京大学, 大学院総合文化研究科, 教授 (90302801)
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| Co-Investigator(Renkei-kenkyūsha) |
HAYASHI Yuuki 東京大学, 大学院総合文化研究科, 助教 (90444059)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 蛋白質 / フォールディング / 天然変性蛋白質 / 分子認識 / NMR |
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| Outline of Final Research Achievements |
Intrinsically disordered proteins (IDPs) have disordered structures under physiological conditions but fold into specific structures upon binding to their target proteins. Because many eukaryotic proteins are IDPs, it is important to elucidate the determinants of the mechanisms of coupled folding and binding of IDPs and to unify the understanding of how IDPs recognize their target molecules. Here, we showed that even a single IDP can contain two regions that bind their targets via different binding mechanisms, including the induced-fit and conformational selection mechanisms. Moreover, our results suggest that the folding ability of IDPs determines their binding mechanisms.
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Report
(4 results)
Research Products
(46 results)
