| Project/Area Number |
23770193
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
OHHASHI Yumiko 独立行政法人理化学研究所, 脳科学総合研究センター, 研究員 (10422669)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | アミロイド / 核磁気共鳴法 / 構造多形 / Sup35 / 天然変性蛋白質 / 部分構造 / 揺らぎ / 核磁気共鳴 / タンパク質 |
|---|
| Research Abstract |
Protein aggregates (amyloid) are common pathological feature of most neurodegenerative diseases. In this study, I investigated the molecular mechanism controlling of determination of amyloid structural polymorphism which affects the clinical state of such diseases, using a yeast prion protein, Sup35. From measurements of several NMR methods focusing on the Sup35 structural fluctuation and local conformation, I found two amyloid initiation sites on Sup35 sequence. Thus, it was conceivable that amyloid structural polymorphism arises from the competition of these two sites. Next, I found the relatively compact local conformation in a part of WT Sup35NM. This result exhibited that the one initiation site is included in this compact area, so another site is advantageous in WT amyloid formation. In conclusion, it was suggested that amyloid structural polymorphism is induced by the destruction of local conformation by amino acid substitution.
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