Analysis of a ADP-bound non-muscle myosin molecule
Project/Area Number |
14580678
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
|
Research Institution | Ninon University |
Principal Investigator |
CHAEN Shigeru Ninon University, Department of Applied Physics, College of Humanities and Sciences, Professor, 文理学部, 教授 (60142452)
|
Co-Investigator(Kenkyū-buntansha) |
MARUTA Shinsaku SOKA University, Department of Bioinformatics, 工学部, 助教授 (40231732)
|
Project Period (FY) |
2002 – 2003
|
Project Status |
Completed (Fiscal Year 2003)
|
Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2003: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2002: ¥2,800,000 (Direct Cost: ¥2,800,000)
|
Keywords | myosin / actin / FENN effect / muscle contraction / single molecule physiology / optical tweezer / アクトミオシン |
Research Abstract |
It has been reported that conformational changes occurred at the light chain portion of smooth muscle myosin and brush border myosin when ADP was added to the actomyosin complex. And the optical tweezer experiment has revealed that the foece generation occurred by two steps, leading the hypothesis that the second step of force is generated by the ADP dissociation. However, the decrease in the force of smooth muscle by adding ADP was not observed. So, the conformational changes seen in the fight chain by ADP is thought to be the strain-dependent ADP dissociation, not a portion of a power stroke. The purpose of this study was to elucidate the strain-dependent ADP dissocation. Unfortunately, a lot of time was spent to develope the experimental apparatus and the method, so the conclusion on the strain-dependent ADP dissociation was not obtained. However, we have made a fine apparatus that measure the force generation of a single myosin molecule from brush border. We describe the process of developing the apparatus, the preparation of the brush border myosin, and the preparation of the beads sample, and show the result of the force generation of single myosin molecule.
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Report
(3 results)
Research Products
(5 results)