Force and velocity measured for single kinesin molecules

Svoboda, K., Block, S. M. (June 1994) Force and velocity measured for single kinesin molecules. Cell, 77 (5). pp. 773-84. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/8205624
DOI: 10.1016/0092-8674(94)90060-4

Abstract

We measured the force-velocity curves of single kinesin molecules attached to silica beads moving in an in vitro motility assay. Optical trapping interferometry was used to track movement with subnanometer precision and to apply calibrated, pN-sized forces to the beads. Velocity decreased linearly with increasing force, and kinesin molecules moved against applied loads of up to 5-6 pN. Comparison of force-velocity curves at limiting and saturating ATP concentrations suggests that the load-dependent diminution in kinesin velocity may be due to a decrease in the net displacement per molecule of ATP hydrolyzed, not simply to a slowing of the ATP turnover rate; kinesin would therefore appear to be a loosely coupled motor.

Item Type: Paper
Uncontrolled Keywords: Adenosine Triphosphate/metabolism Animals Biomechanics Hydrolysis Interferometry Kinesin/chemistry/*metabolism Kinetics Silicon Dioxide Thermodynamics
Subjects: bioinformatics > genomics and proteomics > small molecules > ATP
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > kinesin-5 protein
CSHL Authors:
Communities: CSHL labs > Svoboda lab
Depositing User: Matt Covey
Date: 3 June 1994
Date Deposited: 01 May 2015 20:11
Last Modified: 01 May 2015 20:11
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31472

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