Protein folding study by real-time folding-unfolding proteolysis
| Project/Area Number |
22710215
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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 |
Living organism molecular science
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| Research Institution | Kyoto Prefectural University (2011)
Osaka University (2010) |
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Principal Investigator |
TAKANO Kazufumi 京都府立大学, 大学院・生命環境科学研究科, 教授 (40346185)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
Fiscal Year 2011: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2010: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 生体高分子 / タンパク質 / フォールディング / プロテアーゼ / フォールデング |
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| Research Abstract |
In this work, we examined the slow unfolding pathway of Tk-RNase H2 by pulse proteolysis using a super-stable protease. Through these experiments, we found that Tk-RNase H2 includes two different forms with N-state and N'-state in the native state. The N-state has the large hydrophobic surface in the C-terminal region. In the early stage of unfolding, the N-state changes to an intermediate state(A-state) which is digested by protease at the C-terminal region. In contrast, the N'-state is a protease resistant form. In the slow unfolding pathway, the A-state shifts to the N'-state which gradually unfolds.
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Report
(3 results)
Research Products
(12 results)
