Single-molecule FRET measurement of structural dynamics of intrinsically disordered domain in EGFR
| Project/Area Number |
26440088
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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 | Institute of Physical and Chemical Research |
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Principal Investigator |
Okamoto Kenji 国立研究開発法人理化学研究所, 佐甲細胞情報研究室, 専任研究員 (40402763)
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| Project Period (FY) |
2014-04-01 – 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 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | １分子計測 / FRET / 天然変性蛋白質 / 分子構造変化ダイナミクス / 上皮成長因子受容体分子 / 分子構造ダイナミクス / EGFR / １分子計測 (SMD) / 天然変性タンパク質 / １分子計測(SMD) |
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| Outline of Final Research Achievements |
Structural dynamics of the intrinsically disordered C-tail domain of the epidermal growth factor receptor (EGFR-CT) was investigated by in vitro single-molecule Foerster resonance energy transfer (FRET) measurements using fragment molecules of EGFR-CT. Although imaging experiments could not directly capture very fast structural fluctuation of the intrinsically disordered protein, it detected changes of the FRET distribution dependent on solution condition (ionic strength). Then FRET distributions of diffusing molecules were acquired by burst measurements to investigate dependence on solution conditions. It was found that FRET was dependent rather on denaturant concentration than on ionic strength. The results suggest that the structure of EGFR-CT is principally determined by locally formed secondary structures while structures of intrinsically disordered proteins are generally thought to be affected by charge interactions.
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Report
(5 results)
Research Products
(9 results)
