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Direct observation of kinesin stepping by optical trapping interferometry

Nature volume 365, pages 721–727 (1993)Cite this article

Abstract

Do biological motors move with regular steps? To address this question, we constructed instrumentation with the spatial and temporal sensitivity to resolve movement on a molecular scale. We deposited silica beads carrying single molecules of the motor protein kinesin on microtubules using optical tweezers and analysed their motion under controlled loads by interferometry. We find that kinesin moves with 8-nm steps.

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Author information

Author notes

  1. Christoph F. Schmidt

    Present address: Department of Physics, University of Michigan, Ann Arbor, Michigan, 48109, USA

  2. Steven M. Block: To whom correspondence should be addressed.

Authors and Affiliations

  1. Rowland Institute for Science, 100 Edwin Land Boulevard, Cambridge, Massachusetts, 02142, USA

    Karel Svoboda, Christoph F. Schmidt & Steven M. Block

  2. Committee on Biophysics, Harvard University, Cambridge, Massachusetts, 02138, USA

    Karel Svoboda

  3. Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115, USA

    Bruce J. Schnapp

Authors
  1. Karel Svoboda
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  2. Christoph F. Schmidt
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  3. Bruce J. Schnapp
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  4. Steven M. Block
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Svoboda, K., Schmidt, C., Schnapp, B. et al. Direct observation of kinesin stepping by optical trapping interferometry. Nature 365, 721–727 (1993). https://doi.org/10.1038/365721a0

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