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Direct observation of the binding state of the kinesin head to the microtubule

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  • Nicholas R. Guydosh

    (Biophysics Program,)

  • Steven M. Block

    (Department of Biology,
    Stanford University, Stanford, California 94305, USA)

Abstract

Kinesin in motion Kinesin is a dimeric, processive motor that moves along microtubule filaments taking alternative steps with its two heads. In this study Nicholas Guydosh and Steven Block have developed a single-molecule assay that can directly report head binding and unbinding during kinesin movement. They find that between steps, only one head of kinesin remains bound to the microtubule at low ATP concentrations, while the second head remains unbound and can move around its equilibrium position. Single-molecule techniques developed in this study will be useful for analysing the dynamic properties of other motor proteins.

Suggested Citation

  • Nicholas R. Guydosh & Steven M. Block, 2009. "Direct observation of the binding state of the kinesin head to the microtubule," Nature, Nature, vol. 461(7260), pages 125-128, September.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7260:d:10.1038_nature08259
    DOI: 10.1038/nature08259
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    Cited by:

    1. Ann, Minjung & Lee, Kong-Ju-Bock & Park, Pyeong Jun, 2015. "Stochastic dynamics of coupled active particles in an overdamped limit," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 436(C), pages 126-134.

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