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Coupling of kinesin steps to ATP hydrolysis

Author

Listed:
  • Wei Hua

    (*Biophysics and Structural Biology Graduate Program, Brandeis University)

  • Edgar C. Young

    (Brandeis University)

  • Margaret L. Fleming

    (*The Center for Complex Systems, Brandeis University)

  • Jeff Gelles

    (*The Center for Complex Systems, Brandeis University)

Abstract

A key goal in the study of the function of ATP-driven motor enzymes is to quantify the movement produced from consumption of one ATP molecule1,2,3. Discrete displacements of the processive motor kinesin along a microtubule have been reported as 5 and/or 8 nm (refs 4, 5). However, analysis of nanometre-scale movements is hindered by superimposed brownian motion. Moreover, because kinesin is processive and turns over stochastically, some observed displacements must arise from summation of smaller movements that are too closely spaced in time to be resolved. To address both of these problems, we used light microscopy instrumentation6 with low positional drift (

Suggested Citation

  • Wei Hua & Edgar C. Young & Margaret L. Fleming & Jeff Gelles, 1997. "Coupling of kinesin steps to ATP hydrolysis," Nature, Nature, vol. 388(6640), pages 390-393, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6640:d:10.1038_41118
    DOI: 10.1038/41118
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    Cited by:

    1. Chou, Y.C. & Hsiao, Yi-Feng & To, Kiwing, 2015. "Dynamic model of the force driving kinesin to move along microtubule—Simulation with a model system," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 433(C), pages 66-73.

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