| Project/Area Number |
12680660
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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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 | Tokyo University of Science |
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Principal Investigator |
YAMADA Takenori Tokyo Univ. of Sci., Dept. of Physics, professor, 理学部, 教授 (50027330)
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| Co-Investigator(Kenkyū-buntansha) |
KUNIOKA Yuki Tokyo Univ. of Sci., Dept. of Physics, Asst. Prof., 理学部, 助手 (10318199)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2001: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2000: ¥2,500,000 (Direct Cost: ¥2,500,000)
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| Keywords | myosin / atomic force microscope / single molecule manipulation / single molecule analysis / motor protein / molecular motor / 単一分子計測・操作 / 一分子解析 |
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| Research Abstract |
Muscle contraction takes place by relative sliding motions of actin and myosin filaments. The sliding force is produced by the structural changes of myosin heads (motor protein) extruded from myosin filaments by interacting with actin filaments utilizing the chemical energy of the ATP hydrolysis. However the molecular mechanism of how the force is produced in myosin motor and transmitted at the actin and myosin interface is still unclear
In the present research project, therefore, we investigated in detail the force generating processes of myosin motor at single molecule level. We made two experimental approaches to attack this problem; i.e., (1) whether or not myosin motor can generate force without the interaction with actin filaments and (2) whether or not myosin motor slides straightly along actin filaments
In the first approach, we used recombinant myosin motors prepared by the gene technology.
Transfored at actin binding myopathy loop by the cantilever tip of atomic force microscope
… More
(AFM). Thus the force to be generated by myosin motor and the structural changes to be induced in myosin head could simultaneously be measured based on the deflections of AFM cantilever. The results obtained suggested that myosin motor could generate force without the interaction with actin filaments. In the second approach, small micro-beads coated with myosin filaments were prepared and examined how these second approach, small micro-beads coated with myosin filaments were prepared and examined how these beads slid along actin filaments, they straightly slid along actin filaments. As the number of myosin filaments coated with myosin flaments, they straightly slid along actin filaments. As the number of myosin filaments coated to micro-beads was decreased, sliding motions became non-linear and irregular
These results suggest that the force is produced by the structural changes of myosin motor it self and the produced force is transmitted to the sliding motion, the pattern of which strongly depends on the interaction between myosin motor and actin filaments Less
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