Assessment of effects on deuteration and temperature in protein neutron crystallography
| Project/Area Number |
15K18494
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | National Institutes for Quantum and Radiological Science and Technology (2016)
Japan Atomic Energy Agency (2015) |
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Principal Investigator |
Hirano Yu 国立研究開発法人量子科学技術研究開発機構, 高崎量子応用研究所 東海量子ビーム応用研究センター, 研究員(定常) (80710772)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 蛋白質 / 中性子構造 |
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| Outline of Final Research Achievements |
As a result of the investigation of processing of neutron diffraction data, high quality data were obtained with high-resolution data of high-potential iron-sulfur protein. The high-resolution neutron structure revealed the positions of hydrogen atoms in charged amino acids and solvent molecules on the protein surface. The structure also displayed that the positions of hydrogen atoms are changed depending on the hydrogen bond distances. The high resolution structure analysis will clarify effects of the conditions on neutron data collection. In addition, the high resolution analysis is important for understanding the function and properties of proteins.
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Report
(3 results)
Research Products
(6 results)
