| Project/Area Number |
16K14707
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | Nagoya University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
IKURA Teikichi 東京医科歯科大, 難治疾患研究所, 准教授 (50251393)
HAMADA Daizo 神戸大学, 大学院工学研究科, 特命准教授 (60372132)
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| Research Collaborator |
TENNO Natsuko
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | 分子シールド効果 / 分子夾雑 / 高分子クラウディング / 朝倉・大沢理論 / 天然変性タンパク質 / アミロイド線維 / 化学シフト / アミド水素 / 温度依存性 / 凍結保護 / 凝集抑制 / アミロイド繊維形成 / タンパク質 / 生体分子 / 分子クラウディング / 選択的水和 |
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| Outline of Final Research Achievements |
Macromolecular crowding is the phenomenone that alters the properties of molecules in a solution when high concentrations of macromolecules (molecular crowders) are present. In a living cell, one of the most abundant molecular crowders is the protein itself. We focus on the properties of the intrinsically disordered proteins (IDPs) as a macromolecular crowder. We recently found that IDPs have cryoprotective activity against the other proteins, and we hypothesized that this cryoprotective activity was origined by IDP's molecular shileding effect. For further understanding IDP's molecular shielding effect, aggregation inhibition of IDPs in the other conditions were examined. We found that some IDPs can suppress amyloid formation of Abeta(1-42) peptide.
We have also succeeded in developing the new method to discriminate IDPs from non-IDPs using NMR signal. In detail, chemical shift temperature coefficient (CSTC) of amide protons is a good indication.
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