| Project/Area Number |
18KK0194
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| Research Category |
Fund for the Promotion of Joint International Research (Fostering Joint International Research (B))
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| Allocation Type | Multi-year Fund |
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| Review Section |
Medium-sized Section 43:Biology at molecular to cellular levels, and related fields
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| Research Institution | Hokkaido University |
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Principal Investigator |
Ose Toyoyuki 北海道大学, 先端生命科学研究院, 教授 (80380525)
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| Co-Investigator(Kenkyū-buntansha) |
齋藤 徹 広島市立大学, 情報科学研究科, 講師 (80747494)
塚本 卓 北海道大学, 先端生命科学研究院, 助教 (30744271)
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| Project Period (FY) |
2019-02-07 – 2023-03-31
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| Project Status |
Completed (Fiscal Year 2022)
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| Budget Amount *help |
¥17,680,000 (Direct Cost: ¥13,600,000、Indirect Cost: ¥4,080,000)
Fiscal Year 2021: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2020: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2019: ¥8,840,000 (Direct Cost: ¥6,800,000、Indirect Cost: ¥2,040,000)
Fiscal Year 2018: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
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| Keywords | 結晶学 / 中性子回折 / 水素生物学 / QM/MM MD / 結晶巨大化 / アミン/イミン / ヘテロ芳香環 / Watson-Crick型塩基対 / 中性子 / 結晶回折 / 結晶成長 / 中性子線回折 / アンモニア / 窒素 / 中性子線 / QM/MM-MD |
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| Outline of Final Research Achievements |
Structural biology, in which techniques such as X-ray crystallography, electron microscopy, and NMR are used to analyze the structure of biomolecules, and have been applied even for highly difficult biomolecules. However, such general-purpose methods are not sufficient for identifying hydrogen positions. Neutron diffraction is the most suitable method to analyze hydrogen atoms. We have developed protein crystal growth methods for neutron crystallography; we focus on the interaction between nitrogen atoms and hydrogen atoms. The target proteins are essential to understanding amine and imine hydrogens. Using the newly developed method, we successfully obtained huge crystals suitable for neutron diffraction such as amidotransferase, nucleotide base deaminase, cysteine protease, and antifreeze protein. From the neutron analysis, we identified the presence of an ammonium for the first time. Structural analysis and computational analysis with QM/MM-MD were also performed.
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| Academic Significance and Societal Importance of the Research Achievements |
X線結晶解析，電子顕微鏡，NMR法などの技術を用いて生体高分子構造を明らかにする構造生物学は円熟期を迎え，高難度の事象に対しても数多くの解析が為されている。しかし一方で，水素位置を捉えるためにはこうした汎用法は充分でなく，中性子線解析が最適である。ここでは中性子線回折法のための蛋白質結晶成長法を開発しながら，窒素原子と水素原子の相互作用に注目し，水素を理解することが本質であるものを厳選し，結晶大型化・中性子線構造解析，量子古典混合分子動力学計算（QM/MM-MD）をおこなった。
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