Dynamical structure analysis of intrinsically disordered proteins by neutron scattering using segment deuteration method
| Project/Area Number |
18H02391
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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 43020:Structural biochemistry-related
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| Research Institution | Yokohama City University |
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Principal Investigator |
SATO Mamoru 横浜市立大学, 生命医科学研究科, 教授 (60170784)
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| Co-Investigator(Kenkyū-buntansha) |
小田 隆 立教大学, 理学部, 助教 (00573164)
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| Project Period (FY) |
2018-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥17,680,000 (Direct Cost: ¥13,600,000、Indirect Cost: ¥4,080,000)
Fiscal Year 2020: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2019: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2018: ¥10,270,000 (Direct Cost: ¥7,900,000、Indirect Cost: ¥2,370,000)
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| Keywords | 天然変性タンパク質 / 中性子小角散乱 / セグメント重水素化 |
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| Outline of Final Research Achievements |
In the dynamical structural analysis of proteins by neutron scattering (SANS), neutron facilities overseas were not available at all due to the COVID-19 pandemic. So, X-ray scattering (SAXS) data collected prior to SANS experiment were used for preliminary analysis. The analysis was performed by ensemble optimization method. As a result, the structure of the full-length Hef protein in solution could be well reproduced as an ensemble of six structures with different conformations.
Furthermore, we have established a method for efficient preparation of polypeptide chain ligation by using split intein, NpuDnaE. In addition, a sample preparation protocol in which the deuteration ratio was controlled and a protocol for evaluating the deuteration ratio were also established.
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| Academic Significance and Societal Importance of the Research Achievements |
タンパク質の動的構造の情報は創薬の分野で創薬候補化合物のヒット率の向上に大きく寄与するものと期待され、わが国の国家プロジェクトとして、京／富嶽コンピューターを利用した分子動力学計算で予測されてきた。しかし、これはあくまでもin silicoのシミュレーションの世界の話で、実験データに基づいたタンパク質の動的構造解析法の開発が長く待たれていた。その意味で、当該研究は学術的な意義とともに社会的意義も非常に大きいと期待される。
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] Structure of the UHRF1 Tandem Tudor Domain Bound to a Methylated Non-histone Protein, LIG1, Reveals Rules for Binding and Regulation2019
Author(s)
Kori, S. Ferry, L. Matano, S. Jimenji, T. Kodera, N. Tsusaka, T. Matsumura, R. Oda, T. Sato, M. Dohmae, N. Ando, T. Shinkai, Y. Defossez, P. A. Arita, K.
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Journal Title
Structure
Volume: 27
Issue: 3
Pages: 1-12
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Presentation] The dynamic structure and function of intrinsically disordered region of Hef that is associated with a DNA repair2019
Author(s)
T. Oda, A. Sekino, A. Murakami1, R. Oi, M. Yoneyama, N. Kodera, T. Ando, T. Konuma, K. Sugase, T. Oroguchi, R. Inoue, M. Sugiyama, S. Ishino, Y. Ishino, and M. Sato
Organizer
The 3rd Asia-Oceania Conference on Neutron Scattering 2019 (AOCNS 2019)
Related Report
Int'l Joint Research / Invited
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[Presentation] The structure and function of intrinsically disordered region of Hef that is associated with a DNA repair（DNA修復にかかわるHefの天然変性領域の構造と機能）2019
Author(s)
T. Oda, A. Sekino, A. Murakami, R. Oi, M. Yoneyama, N. Kodera, T. Ando, T. Konuma, K. Sugase, T. Oroguchi, S. Ishino, Y. Ishino, M. Sato
Organizer
第57回日本生物物理学会年会
Related Report
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