Single-molecular analysis of the binding state of myosin v and actin

Yusuke Oguchi*, Adrian O. Olivares, Enrique M. De La Cruz, Shin'ichi Ishiwata

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review


    A class-V myosin, myosin V, one of 18 known classes of actin-based motor proteins, plays a role in transporting organelles within a cell. Unlike myosin-II, which functions as an assembly in the thick filaments of muscle, myosin V is a two-headed processive motor protein, which functions as a single molecule: myosin V performs many consecutive steps before it detaches from an actin filament accompanied by catalytic cycles of ATP (adenosine 5'-triphosphate) ase. The mechanism of such chemomechanical steps is explained by a "Hand-over-hand model" in which two heads of myosin V alternately repeat single-headed and double-headed bindings with an actin filament. To investigate the binding state of myosin V at several key nucleotide states during ATP hydrolysis, we measured the mechanical properties of a single myosin V - actin complex by applying an external load with optical trap.

    Original languageEnglish
    Pages (from-to)239-240
    Number of pages2
    JournalJournal of Physics: Conference Series
    Issue number1
    Publication statusPublished - 2006 Mar 22

    ASJC Scopus subject areas

    • General Physics and Astronomy


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