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Issue 24, 2009
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Multiscale approaches for studying energy transduction in dynein

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Abstract

Cytoplasmic dynein is an important motor that drives all minus-end directed movement along microtubules. Dynein is a complex motor whose processive motion is driven by ATP-hydrolysis. Dynein’s run length has been measured to be several millimetres with typical velocities in the order of a few nanometres per second. Therefore, the average time between steps is a fraction of a second. When this time scale is compared with typical time scales for protein side chain and backbone movements (∼10−9 s and ∼10−5 s, respectively), it becomes clear that a multi-timescale modelling approach is required to understand energy transduction in this protein. Here, we review recent efforts to use computational and mathematical modelling to understand various aspects of dynein’s chemomechanical cycle. First, we describe a structural model of dynein’s motor unit showing a heptameric organization of the motor subunits. Second, we describe our molecular dynamics simulations of the motor unit that are used to investigate the dynamics of the various motor domains. Third, we present a kinetic model of the coordination between the two dynein heads. Lastly, we investigate the various potential geometries of the dimer during its hydrolytic and stepping cycle.

Graphical abstract: Multiscale approaches for studying energy transduction in dynein

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Publication details

The article was received on 30 Jan 2009, accepted on 20 Apr 2009 and first published on 15 May 2009


Article type: Paper
DOI: 10.1039/B902028D
Citation: Phys. Chem. Chem. Phys., 2009,11, 4840-4850
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    Multiscale approaches for studying energy transduction in dynein

    A. W. R. Serohijos, D. Tsygankov, S. Liu, T. C. Elston and N. V. Dokholyan, Phys. Chem. Chem. Phys., 2009, 11, 4840
    DOI: 10.1039/B902028D

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