2015 Fiscal Year Final Research Report
Phyical Chemical Analysis of conformational dynamics of globular proteins
Project/Area Number |
24570181
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Nagoya University |
Principal Investigator |
Maki Kosuke 名古屋大学, 理学(系)研究科(研究院), 准教授 (30361570)
|
Project Period (FY) |
2012-04-01 – 2016-03-31
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Keywords | フォールディング / 蛋白質 / 構造形成 |
Outline of Final Research Achievements |
The specific aim of this study is to understand the mechanisms of protein folding in terms of physical chemistry, by quantitatively representing the structural and energetic characteristics of relevant species. Nonuniform chain collapse was observed in the early folding of staphylococcal nuclease by using ultrarapid mixing methods combined with fluorescence resonance energy transfer, indicating that specific interactions play a major role in forming early folding intermediates. A systematic study on urea-induced folding of apomyoglobin, using ultrarapid mixing methods, revealed that an ensemble of folding intermediates, which transiently accumulates during folding under strongly native conditions, is formed by the same kinetics as the equilibrium intermediate, which stably populated at equilibrium under moderately denaturing conditions, indicating that these molecular species consist of a single molecular species.
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Free Research Field |
生物物理学
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