Structural changes in the neck linker of kinesin explain the load dependence of the motor's mechanical cycle

A. Mogilner, A. J. Fisher, R. J. Baskin

Research output: Contribution to journalArticle

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).

Original languageEnglish (US)
Pages (from-to)143-157
Number of pages15
JournalJournal of Theoretical Biology
Volume211
Issue number2
DOIs
StatePublished - Jul 21 2001

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Kinesin
kinesin
Structural Change
neck
Neck
Adenosinetriphosphate
Cycle
Experimental Data
Motility
Microtubules
Adenosine Triphosphate
Nucleotides
Kinetics
Molecules
Model
microtubules
Proteins
Protein
Theoretical Models
Dependent

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

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Structural changes in the neck linker of kinesin explain the load dependence of the motor's mechanical cycle. / Mogilner, A.; Fisher, A. J.; Baskin, R. J.

In: Journal of Theoretical Biology, Vol. 211, No. 2, 21.07.2001, p. 143-157.

Research output: Contribution to journalArticle

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