Analysis of the mechanism of protein aggregation at an atomic level and development of a method of stabilizing it by chemical modification
| Project/Area Number |
25440069
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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 | Yokohama City University (2014-2016)
Osaka University (2013) |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | 核磁気共鳴 / 蛋白質 / 立体構造解析 / 非特異的相互作用 / NMR / 凝集 / 疎水的相互作用 / 安定性 / 単分散 / 磁気緩和速度 / 緩和分散 |
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| Outline of Final Research Achievements |
There are many examples of proteins interacting with each other while maintaining their specific three-dimensional structures, and leading to aggregation. Such aggregation is also associated with many kinds of diseases. It is also one of the causes that hinder detailed spectroscopic analyses such as NMR. The purpose of this study is to study the physical mechanism by which such aggregation occurs spontaneously and to develop chemical modification methods that inhibit it. I have targeted VanX, an enzyme involved in vancomycin resistance in Enterococci. The tertiary structure as a dimer was analyzed mainly by NMR. As a result, it was shown that VanX aggregates to tetramers as the concentration increases. It was also found that the degree of aggregation changes depending on the solvent pH.
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Report
(5 results)
Research Products
(8 results)
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[Journal Article] Intrinsic disorder mediates cooperative signal transduction in STIM12014
Author(s)
Furukawa, Y., Teraguchi, S., Ikegami, T., Dagliyan, O., Jin, L., Hall, D., Dokholyan, N.V., Namba, K., Akira, S., Kurosaki, T., Baba, Y., Standley, D.M.
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Journal Title
J Mol Biol
Volume: 426
Issue: 10
Pages: 2082-97
DOI
Related Report
Peer Reviewed / Open Access
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