Visualization of rotation of ATP synthase driven by proton motive force using single-molecule techniques and microdevices
Project/Area Number |
21770168
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Biophysics
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Research Institution | Osaka University |
Principal Investigator |
IINO Ryota Osaka University, 産業科学研究所, 助教 (70403003)
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Project Period (FY) |
2009 – 2010
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Project Status |
Completed (Fiscal Year 2010)
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Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2010: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2009: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
|
Keywords | 1分子計測・操作 / 回転分子モーター / 分子モーター / 1分子計測 / 1分子イメージング / ATP合成酵素 / 基板支持脂質二重膜 / パッチクランプ / マイクロデバイス / プロトン駆動力 / 膜タンパク質 |
Research Abstract |
We have tried to directly observe the rotation of ATP synthase driven by proton motive force. ATP synthase was reconstituted into the lipid bilayer membrane supported on the solid substrate such as NTA-agarose and NTA-acrylamide. Electric sealing of and voltage allocation to the supported membrane were examined using pipette made by glass or polydimethylsiloxane. Several tens of mega ohm resistance was achieved, and used to seal the membrane containing the rotating ATP synthase driven by ATP hydrolysis. Some of ATP synthase showed change in the rotation speed when voltage was applied. We need elaborate control experiments to confirm whether the change really reflects the behavior of the ATP synthase.
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Report
(3 results)
Research Products
(53 results)
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[Journal Article] Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators2009
Author(s)
Imamura, H., Huynh Nhat, K.P., Togawa, H., Saito, K., Iino, R., Kato-Yamada, Y., Nagai, T., Noji, H.
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Journal Title
Proc Natl Acad Sci USA. 106
Pages: 15651-15656
Related Report
Peer Reviewed
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