Dynamic study on three SH3 domain proteins, mainly consisted by beta structures
| Project/Area Number |
20540400
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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/Chemical physics
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| Research Institution | Kansai Medical University |
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Principal Investigator |
KIHARA Hiroshi Kansai Medical University, 医学部, 教授 (20049076)
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| Co-Investigator(Kenkyū-buntansha) |
SHINJO Masaji 関西医科大学, 医学部, 助教 (90388447)
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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 |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥130,000 (Direct Cost: ¥100,000、Indirect Cost: ¥30,000)
Fiscal Year 2009: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2008: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | フォールディング / フォールディング初期中間体 / クライオストップトフロー法 / SH3ドメイン蛋白質 / SH3 / 蛋白質のフォールディング / PI3K SH3 / アミロイド線維形成 / α-ヘリックスの多い初期中間体 / X線溶液散乱 / src SH3 / βラクトグロブリン / αヘリックス / 円偏光二色性 |
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| Research Abstract |
Folding process of three homologous SH3 proteins (src, Fyn and PI3K domain proteins) were monitored by cryo-stopped-flow method combined with circular dichroism (CD),fluorescence and X-ray scattering. Results show that the folding pathways are different from each other, though the native tertiary structures are similar with each other. Transiently appeared intermediate of src SH3 are rich in alpha-helix. Its structure was calculated by two programs, GASBOR and SAXS-MD. Both structures are similar at least in terms of gross conformation. The intermediate calculated by SAXS-MD shows atomic coordinates which gives us main chain conformation in the transiently appearing structure.
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Report
(4 results)
Research Products
(42 results)
