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, 211 (2), 143-57

Structural Changes in the Neck Linker of Kinesin Explain the Load Dependence of the Motor's Mechanical Cycle

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Structural Changes in the Neck Linker of Kinesin Explain the Load Dependence of the Motor's Mechanical Cycle

A Mogilner et al. J Theor Biol.

Abstract

The two-headed motor protein kinesin hydrolyzes ATP and moves on microtubule tracks towards the plus end. The motor develops speeds and forces of the order of hundreds of nanometers per second and piconewtons, respectively. Recently, the dependence of the velocity, the dissociation rate and the displacement variance on the load and the ATP concentration were measured in vitro for individual kinesin molecules (Coppin et al., 1997; Visscher et al., 1999) over a wide range of forces. The structural changes in the kinesin motor that drive motility were discovered by Rice et al. (1999). Here we present a phenomenological model for force generation in kinesin based on the bi-stable, nucleotide-dependent behavior of the neck linker. We demonstrate that the model explains the mechanical, kinetic and statistical (experimental) data of Coppin et al. (1997). We also discuss the relationship between the model results and experimental data of Visscher et al. (1999).

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Cited by 2 PubMed Central articles

  • Regular Gaits and Optimal Velocities for Motor Proteins
    RE DeVille et al. Biophys J 95 (6), 2681-91. PMID 18556760.
    It has been observed in numerical experiments that adding a cargo to a motor protein can regularize its gait. Here we explain these results via asymptotic analysis on a g …
  • Kinesin: A Molecular Motor With a Spring in Its Step
    N Thomas et al. Proc Biol Sci 269 (1507), 2363-71. PMID 12495505. - Review
    A key step in the processive motion of two-headed kinesin along a microtubule is the 'docking' of the neck linker that joins each kinesin head to the motor's dimerized co …

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