2013 Fiscal Year Final Research Report
Physical basis for the molecular recognition by intrinsically disordered proteins
| Project/Area Number |
23570188
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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, 総合文化研究科, 准教授 (90302801)
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| Project Period (FY) |
2011 – 2013
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| Keywords | 蛋白質 / フォールディング / 分子認識 / 天然変性蛋白質 |
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| Research Abstract |
Intrinsically disordered proteins (IDPs) have disordered structures in isolation but fold into specific structures upon binding to their partner molecules. Because 40% of eukaryotic proteins are considered to be IDPs, elucidation of the mechanism of molecular recognition by IDPs has been one of the crucial issues in biophysics. Here, we investigated the mechanisms of molecular recognition by IDPs using NMR and other techniques. We found that IDPs can recognize partner molecules very rapidly and that both the induced-fit and the conformational selection mechanisms are utilized in the recognition of partner molecules depending on IDPs.
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[Journal Article] Flexible and rigid structures in HIV-1 p17 matrix protein monitored by relaxation and amide proton exchange with NMR2014
Author(s)
Ohori, Y., Okazaki, H., Watanabe, S., Tochio, N., Arai, M., Kigawa, T., & Nishimura, C.
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Journal Title
Biochim. Biophys. Acta
Volume: 1844(3)
Pages: 520-526
DOI
Peer Reviewed
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[Journal Article] Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence2013
Author(s)
Oikawa, H., Suzuki, Y., Saito, M., Kamagata, K., Arai, M., & Takahashi, S.
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Journal Title
Scientific Reports
Volume: 3
Pages: 2151
DOI
Peer Reviewed
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