2022 Fiscal Year Final Research Report
Exploring Molecular Mechanisms for Creating Diverse Functions based on Common Structures
| Project/Area Number |
20H02693
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Review Section |
Basic Section 32010:Fundamental physical chemistry-related
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| Research Institution | Osaka University |
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Principal Investigator |
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| Project Period (FY) |
2020-04-01 – 2023-03-31
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| Keywords | アロステリー / ラマン分光法 / タンパク質ダイナミクス |
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| Outline of Final Research Achievements |
The difficulty in studying the physical chemistry of proteins lies in the diversity of protein structures and functions, making it difficult to find universal principles. Therefore, in this study, we focused on the common structure of proteins. Some rhodopsins selectively transport a variety of ions, including protons, sodium ions, and chloride ions, on a common three-dimensional structural basis. In addition, many oxygen-carrying proteins have a common subunit structure called globin fold but exhibit cooperativity through diverse fashions of association. These facts indicate that the common structure is the basis of the function and strongly suggest that functional diversity is caused by regulation based on the common structure. Therefore, we compared and clarified the functional mechanisms of a group of proteins that share a common structure but exhibit different functions or different association fashions.
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| Free Research Field |
生物物理化学
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| Academic Significance and Societal Importance of the Research Achievements |
化学の進展によって、化学者はある機能を持った分子を設計し、それを実際に合成することができるようになった。しかし、複数の機能単位を組み合わせ、互いに連動する、より高度な機能分子を創ることはいまだに困難である。それは合成の技術的な難しさのためではなく、連動させる原理がわからないためであり、原理がわからなければ設計のしようがないためである。「連動性を生む必要十分条件は何か？」を理解できれば、連動性をもった機能性分子を設計するための重要な知見が得られる。連動性の理解は分子機能にとって本質的な問題であり、分子の理解と制御に重要な貢献を果たす。
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