Structure Study of β2m Amyloid Fibril using Dynamic Nuclear Polarization-Enhanced High-Sensitivity Solid-State NMR
| Project/Area Number |
21870019
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Structural biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
MATSUKI Yoh Osaka University, 蛋白質研究所, 助教 (70551498)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥2,756,000 (Direct Cost: ¥2,120,000、Indirect Cost: ¥636,000)
Fiscal Year 2010: ¥1,313,000 (Direct Cost: ¥1,010,000、Indirect Cost: ¥303,000)
Fiscal Year 2009: ¥1,443,000 (Direct Cost: ¥1,110,000、Indirect Cost: ¥333,000)
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| Keywords | アミロイド繊維 / 固体NMR / 動的核分極 / 希薄サンプリング / β2m / 動的核分極(DNP)法 / 時間-周波数領域情報統合分光(SIFT)法 |
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| Research Abstract |
In this study, (1) more than 200-fold sensitivity enhancement was established for solid-state NMR spectroscopy using Dynamic Nuclear Polarization (DNP). (2) Application of the sparse data sampling technique enabled to detect conventionally unobservable signals. (3) A use of reserve isotope labeling technique resolved many previously unseen signals. (4) A new scheme to detect the molecular interfaces within a fibril was developed for high-selectivity and sensitivity. (5) ss2m was suggested to largely retain its native fold in the fibril, contrary to the widespread belief that amyloid fibril formation generally requires native proteins to adopt a fibril-specific fold.
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Report
(3 results)
Research Products
(8 results)
