2010 Fiscal Year Final Research Report
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
|
Keywords | 1分子計測・操作 / 回転分子モーター |
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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Research Products
(25 results)