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The molecular motor actin-myosin on a substrate

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Transport and Structure

Part of the book series: Lecture Notes in Physics ((LNP,volume 532-532))

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Abstract

Following a short review of the biological function and the structure of molecular motors, we discuss the state of the art of research on the molecular motor actin-myosin. We show how the so called motility assay can been improved by the use of antibodies, yielding clean and reproducible data of the speed of actin on a myosin coated surface. We discuss the dependence of the measured speed on parameters such as ATP concentration, myosin density and temperature; we furthermore show that the specific anchoring of the myosin molecule to the substrate is important for a clean measurement. Using PMMA (poly(methylmethacrylate)) gratings as guidance for the moving actin filaments, we are able to control the mechanical load of the motor via an electric field and to establish a force-speed diagram. The numerical values of duty ratio, internal friction and stalling force of the motor can be deduced from it. The observation of an instability of the motor around stalling conditions is particularly surprising and suggests the existence of a dynamic phase transition.

UMR 168 du CNRS, associé à l’Université Paris 7

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Authors and Affiliations

  1. Laboratoire PhysicoChimieCurie, Institut Curie, 11 rue Pierre et Marie Curie, 75231, Paris Cedex 05, France

    A. Ott

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  1. A. Ott
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Stefan C. Müller Jürgen Parisi Walter Zimmermann

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© 1999 Springer-Verlag

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Ott, A. (1999). The molecular motor actin-myosin on a substrate. In: Müller, S.C., Parisi, J., Zimmermann, W. (eds) Transport and Structure. Lecture Notes in Physics, vol 532-532. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0104220

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  • DOI: https://doi.org/10.1007/BFb0104220

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-66632-5

  • Online ISBN: 978-3-540-48070-9

  • eBook Packages: Springer Book Archive

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