Coupling of kinesin steps to ATP hydrolysis

Wei Hua, Edgar C. Young, Margaret L. Fleming () and Jeff Gelles
Additional contact information
Wei Hua: *Biophysics and Structural Biology Graduate Program, Brandeis University
Edgar C. Young: Brandeis University
Margaret L. Fleming: *The Center for Complex Systems, Brandeis University
Jeff Gelles: *The Center for Complex Systems, Brandeis University

Nature, 1997, vol. 388, issue 6640, 390-393

Abstract: Abstract A key goal in the study of the function of ATP-driven motor enzymes is to quantify the movement produced from consumption of one ATP molecule1,2,3. Discrete displacements of the processive motor kinesin along a microtubule have been reported as 5 and/or 8 nm (refs 4, 5). However, analysis of nanometre-scale movements is hindered by superimposed brownian motion. Moreover, because kinesin is processive and turns over stochastically, some observed displacements must arise from summation of smaller movements that are too closely spaced in time to be resolved. To address both of these problems, we used light microscopy instrumentation6 with low positional drift (

Date: 1997
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/41118 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:388:y:1997:i:6640:d:10.1038_41118

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/41118

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().