Ligand recognition of intrinsically disordered protein revealed by a new single-molecule measurement
| Project/Area Number |
21770173
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | Tohoku University |
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Principal Investigator |
KAMAGATA Kiyoto Tohoku University, 多元物質科学研究所, 助教 (90432492)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
Fiscal Year 2010: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2009: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 変性蛋白質 / 一分子観察 / ダイナミクス / チトクロムc / フォールディング / 天然変性タンパク質 / 一分子蛍光観察 / 基質 / 一分子測定 / イメージング / 天然変性蛋白質 |
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| Research Abstract |
We developed a new single-molecule fluorescence method to investigate folding and dynamics with functions of proteins including ligand-recognition of an intrinsically disordered protein. At first, to understand a physiological property of a denatured protein, we applied our method to obtain the fluorescence fluctuations of two denatured cytochrome c. The fluorescence traces show multiple conformations with the lifetime of ～100ms in denatured proteins. Second, we investigated ligand-binding kinetics of maltose binding protein at a single molecule level. The single-molecule data shows fluctuations between open and close conformations with ～100ms time scale in the absence of maltose. The comparison of its binding rate with the rate of the fluctuations suggests that the ligand-binding of this protein is explained by induced fit model. The application of our developed method to intrinsically disordered proteins will reveal their ligand-recognition process.
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Report
(3 results)
Research Products
(50 results)
