| Project/Area Number |
17K07361
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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 | Kyoto University |
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Principal Investigator |
Inoue Rintaro 京都大学, 複合原子力科学研究所, 准教授 (80563840)
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| Project Period (FY) |
2017-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2019: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2018: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2017: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | 小角中性子散乱 / アルファークリスタリン / 重水素化 / クリスタリン / 中性子散乱 / アルファクリスタリン |
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| Outline of Final Research Achievements |
In this work, we have studied the relationship between the structure and function of alpha -crystallin through the complementary use of analytical ultacentrifuge and deuteration- assisted neutron scattering. In the case of alpha-crystallin hetro-oligomer that consists of alpha A and alpha B subunit, difference of exchange rate between alpha A and alpha B subunit was experimentally clarified. As for the subunit exchange rate under semi-concentrated system, its exchange rate was same as that of dilute one. From the analytical ultacentrifuge measurements, the coexistence of monomer and oligomer was observed regardless of protein concentration. Then, we assumed a model monomer association/disscociation model and succeeded to reproduce the experimental results with this model. Finally, it was concluded that such monomer was responsible for its function.
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| Academic Significance and Societal Importance of the Research Achievements |
近年では、明確な四次構造を持たないタンパク質こそが高等生物の機能を司っていると考えられているが、その機能と構造を結びつける手法が十分には確立していなかった。そこで、本研究課題で培った重水素化支援小角中性子散乱と分析超遠心法の組み合わせは非常に動的な構造を有するタンパク質の特徴づける非常に有効な手法であることが明らかとなった。本手法は他のsmall heat shock proteinのみならずより動的な構造を有する天然変性タンパク質にも適用できると期待できる。
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