NMR analysis of amyloid beta-oligomer by using molecular chaperone encapsulation system.
| Project/Area Number |
23570192
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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 |
MASARU Hoshino 京都大学, 薬学研究科(研究院), 准教授 (70304053)
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| Co-Investigator(Renkei-kenkyūsha) |
IKEGAMI Takahisa 大阪大学たんぱく質研究所, 准教授 (20283939)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | フォールディング / 分子シャペロン / シャペロニン / 核磁気共鳴 / アミロイドβ / GroE / NMR / アミロイド / 可溶性オリゴマー / ＮＭＲ / 構造解析 |
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| Research Abstract |
Nuclear magnetic resonance spectroscopy is a powerful tool for the analysis of protein structure and dynamics in solution. This technique is, however, not able to analyze aggregated proteins and proteins which is in equilibrium in association and dissociation. To circumvent this major disadvantage, it is effective to encapsulate the target protein into the 'cage' composed of molecular chaperone from Escherichia coli. As a first step of the development of molecular chaperone encapsulating system, the long term stability of the molecular chaperone capsule was analyzed by using a green fluorescence protein as a model substrate.
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Report
(4 results)
Research Products
(30 results)
