Structural and functional characteristics of natively unfolded protein
| Project/Area Number |
21570113
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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 |
Structural biochemistry
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| Research Institution | Tottori University |
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Principal Investigator |
KAWATA Yasushi 鳥取大学, 大学院・工学研究科, 教授 (40177697)
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| Co-Investigator(Renkei-kenkyūsha) |
MIZOBATA Tomohiro 鳥取大学, 大学院・工学研究科, 准教授 (50263489)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2010: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2009: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | タンパク質 / 蛋白質 / GroEL / アミロイド線維 / 天然変性 / シャペロニン / αシヌクレイン / 生体分子 / 天延変性 / 細胞毒性 |
|---|
| Research Abstract |
In order to understand the relationship between flexibility and function of protein, we investigated intrinsically disordered protein, alpha-synuclein and molecular chaperone, chaperonin in detail from protein chemistry, biochemistry, and biophysical chemistry points of view. We found that the intrinsic flexibility, structural property, and structural changes of polypeptide triggered amyloid fibril formation and also were involved in the function closely.
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Report
(4 results)
Research Products
(39 results)
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[Presentation] アントシアニンによる神経変性病原因タンパク質のアミロイド線維形成抑制に関するin vitroとin vivo研究2011
Author(s)
河田康志, 鎌田光博, 渡辺保裕, 小林真菜, 吉田早穂, 田村哲也, 本郷邦広, 溝端知宏, 三浦典正, 中島健二, 小林沙織
Organizer
第84回日本生化学会大会
Place of Presentation
京都
Year and Date
2011-09-24
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