2019 Fiscal Year Final Research Report
Studies on the transition state of protein folding by means of correlation analysis between the folding rate and the native structure
Project/Area Number |
16K07314
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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 | The University of Tokyo |
Principal Investigator |
Kuwajima Kunihiro 東京大学, 大学院理学系研究科(理学部), 名誉教授 (70091444)
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Project Period (FY) |
2016-04-01 – 2020-03-31
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Keywords | フォールディング / 速度論 / 遷移状態 |
Outline of Final Research Achievements |
In this study, (1) a standardized protein folding database, in which the folding rate constant of all listed proteins are calculated at the standard temperature (25°C), has been constructed and opened on the internet homepage. (2) The correlations between the Φ values, which represent the degree of structural formation in the transition state of folding, and different structure-based properties of proteins were analyzed, and the relationships between the structure-based properties and the critical structure in the transition state were discussed. (3) Academic literatures concerning the relationships between the folding rate constant and various structure-based properties were investigated, and it has been found that the two-state and the non-two-state folding reactions of proteins apparently seem very different, but are based on essentially the same physical principles.
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Free Research Field |
生物物理学
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Academic Significance and Societal Importance of the Research Achievements |
蛋白質フォールディング機構の研究は,蛋白質の間違ったフォールディングによって引き起こされる,ヒトの様々なフォールディング病(アルツハイマー病,白内障,クロイツフェルト・ヤコブ病,パーキンソン病,II型糖尿病など多数)などの原因解明や治療法の構築の応用研究に役立つと期待される,基盤的な研究である。本研究で構築されたデータベースは,蛋白質フォールディングの計算機シミュレーションや理論研究の研究者によって,広く活用されることが期待される。本研究で実施された,Φ値やフォールディング速度と構造特性との間の相関解析は,本データベースを活用するための事例研究として用いることも出来る。
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