title: Structural changes in the neck linker of kinesin explain the load dependence of the motor's mechanical cycle.
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).
authors: Department of Mathematics and Institute of Theoretical Dynamics, University of California at Davis, CA 95616, USA.
authors: A
authors: A
authors: Mogilner
authors: A J
authors: AJ
authors: Fisher
authors: R J
authors: RJ
authors: Baskin
mesh_terms: D000244:Adenosine Diphosphate / Q000502:physiology; D000255:Adenosine Triphosphate / Q000502:physiology; D000818:Animals; D016547:Kinesins / Q000737:chemistry / Q000502:physiology*; D008870:Microtubules / Q000502:physiology*; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000502:physiology*; D014404:Tubulin / Q000502:physiology*
chemical_list: D020409:Molecular Motor Proteins; D014404:Tubulin; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D016547:Kinesins