Overdamped mechanical model of myosin II

Authors

  • András Bibó
    Affiliation

    Institute of Nuclear Techniques, Budapest University of Technology and Economics

  • Mihály Kovács
    Affiliation

    ELTE–MTA “Momentum” Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University

  • György Károlyi
    Affiliation

    Institute of Nuclear Techniques, Budapest University of Technology and Economics

https://doi.org/10.3311/PPci.2137

Abstract

Due to their small size molecular systems are often overdamped and they are affected by significant fluctuations due to thermal forces. In this paper we investigate the effect of overdamping on a simple mechanical model of myosin II, the motor protein responsible for muscle contraction. We demonstrate that this model, based on the experimentally observed shape of the protein’s subdomains, is consistent with the available experimental results. We also shed new light on the debate whether the powerstroke is a sudden conformational change followed by relaxation to equilibrium or a thermal fluctuation followed by a fixation by a ratchet-like mechanism in an energetically favourable conformation: we propose that these mechanisms coexist.

Keywords:

Myosin II; muscle model; motor protein

Published Online

2013-06-03

How to Cite

Bibó, A., Kovács, M., Károlyi, G. “Overdamped mechanical model of myosin II”, Periodica Polytechnica Civil Engineering, 57(1), pp. 11–19, 2013. https://doi.org/10.3311/PPci.2137

Issue

Section

Research Article