2011 Fiscal Year Final Research Report
Study of motile mechanism of myosin VI using high-speed atomic force microscopy
| Project/Area Number |
22870011
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | Kanazawa University |
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Principal Investigator |
KODERA Noriyuki 金沢大学, バイオAFM先端研究センター, 准教授 (30584635)
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| Project Period (FY) |
2010 – 2011
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| Keywords | ミオシン / アクチン / モータータンパク質 / 一分子計測・操作 / 原子間力顕微鏡 |
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| Research Abstract |
Myosin 6 is the only myosin among myosin superfamily that moves to the minus end of actin filament. Interestingly, it is known that myosin 6 walks with larger stride than that expected from their foot length. However, their functional mechanism has not been elucidated yet, due to the lack of structural evidence. Here, we performed high-speed atomic force microscopy to directly observe their structural dynamics of myosin 6 at work. Then, the structural evidence was successively obtained for the first time, leading to better understanding the functional mechanism of myosin 6.
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[Journal Article] High-speed atomic force microscopy techniques for observing dynamic biomolecular processes.2010
Author(s)
Yamamoto, D., Uchihashi, T., Kodera, N., Yamashita, H., Nishikori, S., Ogura, T., Shibata, M. & Ando, T.
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Journal Title
Methods in Enzymol
Volume: 475
Pages: 541-564
Peer Reviewed
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[Presentation] Direct visualization of intrinsically disordered proteins PQBP-1, MeCP2, andFliK using high-speed atomic force microscopy2011
Author(s)
森哲哉,古寺哲幸,水野志乃,相沢慎一,水口峰之, Szerlong, H., Porter-Goff, M., Hansen, J. C.,安藤敏夫
Organizer
第49回日本生物物理学会年会
Place of Presentation
兵庫県立大学姫路書写キャンパス(兵庫県).
Year and Date
20110916-18
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