Exploring the free energy landscape of the folding and the intermediate ensemble of globular proteins.
| Project/Area Number |
20570153
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Nagoya University |
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Principal Investigator |
MAKI Kosuke Nagoya University, 理学研究科, 准教授 (30361570)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2009: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2008: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 蛋白質 / フォールディング / 速度論 / 連続フロー法 / スタフィロコッカル・ヌクレアーゼ / エネルギー地形 / トリプトファン変異体 |
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| Research Abstract |
The folding mechanisms of two globular proteins, staphylococcal nuclease and horse apomyoglobin, were investigated by using the ultrarapid mixing technique combined with the mutation analysis. Staphylococcal nuclease molecules were found to be already compact within the β-barrel domain several millisecond after the initiation of the folding reaction. Apomyoglobin accumulated at least one intermediate 100 microseconds after the initiation of the folding reaction, followed by the accumulation of at least two intermediate in the sequential pathway, before reaching the native state.
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Report
(4 results)
Research Products
(17 results)
