COORDINATED HYDROLYSIS EXPLAINS THE MECHANICAL-BEHAVIOR OF KINESIN

Authors
Citation
Cs. Peskin et G. Oster, COORDINATED HYDROLYSIS EXPLAINS THE MECHANICAL-BEHAVIOR OF KINESIN, Biophysical journal, 68(4), 1995, pp. 202-211
Citations number
20
Categorie Soggetti
Biophysics
Journal title
ISSN journal
00063495
Volume
68
Issue
4
Year of publication
1995
Supplement
S
Pages
202 - 211
Database
ISI
SICI code
0006-3495(1995)68:4<202:CHETMO>2.0.ZU;2-S
Abstract
The two-headed motor protein kinesin hydrolyzes nucleotide to move uni directionally along its microtubule track at speeds up to 1000 nm/s (S axton 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 a nd Block, 1994a; Svoboda et al., 1994b). We present a model for force generation in kinesin in which the ATP hydrolysis reactions are coordi nated with the relative positions of the two heads. The model explains the experimental data and permits us to study the relative roles of B rownian motion and elastic deformation in the motor mechanism of kines in.