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Coordinated hydrolysis explains the mechanical behavior of kinesin.

Authors
  • Peskin, C S
  • Oster, G
Type
Published Article
Journal
Biophysical journal
Publication Date
Apr 01, 1995
Volume
68
Issue
4 Suppl
Identifiers
PMID: 7787069
Source
Medline
License
Unknown

Abstract

The two-headed motor protein kinesin hydrolyzes nucleotide to move unidirectionally along its microtubule track at speeds up to 1000 nm/s (Saxton et al., 1988) and develops forces in excess of 5 pN (Hunt et al., 1994; Svoboda et al., 1994a). Individual kinesin molecules have been studied recently in vitro, and their behavior has been characterized in terms of force-velocity curves and variance measurements (Svoboda and Block, 1994a; Svoboda et al., 1994b). We present a model for force generation in kinesin in which the ATP hydrolysis reactions are coordinated with the relative positions of the two heads. The model explains the experimental data and permits us to study the relative roles of Brownian motion and elastic deformation in the motor mechanism of kinesin.

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