Raman optical activity measurement of reaction intermediate of photoreceptor proteins and its application
Project/Area Number |
18K05037
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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 |
Review Section |
Basic Section 32010:Fundamental physical chemistry-related
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Research Institution | Saga University |
Principal Investigator |
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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 |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2020: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2019: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2018: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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Keywords | ラマン光学活性 / 光受容タンパク質 / 低温ラマン分光法 / 低温生物学 / 光受容性タンパク質 / 反応中間体 |
Outline of Final Research Achievements |
This research aimed to utilize Raman optical activity (ROA) spectroscopy for the measurement of the three-dimensional (3D) structure of the reaction intermediates in photoreceptor proteins. We chose the photoreceptors, such as light-driven ion pumps, of micro-organisms and planned to measure ROA of their initial photointermediates trapped at low temperature. As the important step for this ROA measurement, we could measured the low-temperature Raman spectra of the initial intermediates of various photoreceptors and studied their early-time structural changes in the photoreactions. We found a couple of photoreceptors, to which the ROA spectroscopy can be applied, and worked on the development of the low-temperature ROA spectrometer.
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Academic Significance and Societal Importance of the Research Achievements |
本研究で実施した光受容タンパク質の極低温ラマン測定は、世界的にみても行える研究グループがほとんど無く、独自性の高い構造情報に基づいた光受容タンパク質の研究成果である。また、ラマン光学活性(ROA)分光法は、今日広く利用されるどの分光手法でも測定ができない、タンパク質の反応サイトの詳細な立体構造を捉えられる方法である。本研究はタンパク質研究において"今まで見えなかった構造を観測する"新展開を拓く取り組みである。
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Report
(4 results)
Research Products
(27 results)
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[Journal Article] Low-temperature Raman spectroscopy of sodium-pump rhodopsin from Indibacter alkaliphilus: Insight of Na+ binding for active Na+ transport2021
Author(s)
Nakamizo, Y., Fujisawa, T., Kikukawa, T., Okamura, A., Baba, H., Unno, M.
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Journal Title
Phys. Chem. Chem. Phys.
Volume: 23
Issue: 3
Pages: 2072-2079
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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