Single molecule reaction analysis of P-types ATPase using electrochemical fast-scanning atomic force microscopy
| Project/Area Number |
22770148
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | University of Tsukuba |
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Principal Investigator |
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2010: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | P 型ATPase / SERCA / Na+-Pump / 高速AFM / 一分子解析 / 高速原子間力顕微鏡 / P型ATPase / 筋小胞体カルシウムポンプ / ナトリウムポンプ / 一分子反応解析 / 電気生理 |
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| Research Abstract |
Ion pumps transport specific cationic ion across the biomembrane against a concentration gradient through the energy obtained from ATP hydrolysis. Recent progresses in crystallographic study of sarcoplasmic reticulum Ca^<2+>-ATPase (SERCA), which is one of the best-characterized P-type ATPases, allow us to discuss the transport mechanisms involving dynamical structural changes of P-type ATPases.
In this study, we constructed a novel method to analyze molecular reaction of P-type ATPase at a single molecular level and real time scale using a newly developed fast-scanning atomic force microscopy. Using the system, we succeeded to observe single molecule of SERCA and plasma membrane sodium pump act as a pumping machine by direct detection of their repeatedly up-and-down conformational changes.
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Report
(3 results)
Research Products
(12 results)
