| Project/Area Number |
13480213
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | TOHOKU UNIVERSITY |
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Principal Investigator |
HIGUCHI Hideo Tohoku University, Graduate school of Engineering, Associate Professor, 大学院・工学研究科, 助教授 (90165093)
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| Project Period (FY) |
2001 – 2003
|
| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥13,700,000 (Direct Cost: ¥13,700,000)
Fiscal Year 2003: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 2002: ¥4,900,000 (Direct Cost: ¥4,900,000)
Fiscal Year 2001: ¥6,700,000 (Direct Cost: ¥6,700,000)
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| Keywords | kinesin / motor protein / single molecules / micro scope |
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| Research Abstract |
Movement is a fundamental charlatanistic of all living things. This is a biogenic function that is attributed to the molecular motors such as kinesin, dynein and myosin. Molecular motors generate forces by using chemical energy derived from the hydrolysis reaction of ATP molecules. Despite a large number of studies on this topic, the chemomechanical energy transduction mechanism still remains unsolved. In this study, the chemomechanical coupling of the ATPase cycle to the mechanical events has been examined for the molecular motor kinesin using single molecule detection (SMD) techniques. The SMD techniques allowed the detection of the movement of single kinesin molecules along a microtubule and showed that kinesin moves in a stepwise manner. Kinesin steps mainly in the forward direction, but occasionally in the backward direction, indicating that the stepping motion is determined by stochastic processes. The stepwise movement is essentially driven by Brownian motion biased in the forward direction and is caused by the interaction between kinesin and the microtubule, which can be dynamically changed by the free energy of ATP hydrolysis.
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