"Gliding Assays" for Motor Proteins: A Theoretical Analysis

Thomas Duke, Timothy E. Holy, and Stanislas Leibler
Phys. Rev. Lett. 74, 330 – Published 9 January 1995
PDFExport Citation

Abstract

Much information about the workings of molecular motors can be gleaned from motility assays in which cytoskeletal filaments are observed as they glide across a surface coated with motor proteins. The statistical properties of the paths followed by the filaments depend both on the motors (their surface concentration and mode of action) and on the filaments (their length and rigidity). By analyzing the dynamics of this system, we determine these dependencies and suggest how they may be used to infer more accurate quantitative information about motor proteins than is currently extracted from gliding assays.

  • Received 2 May 1994

DOI:https://doi.org/10.1103/PhysRevLett.74.330

©1995 American Physical Society

Authors & Affiliations

Thomas Duke, Timothy E. Holy, and Stanislas Leibler

  • Departments of Physics and Molecular Biology, Princeton University, Princeton, New Jersey 08544

References (Subscription Required)

Click to Expand
Issue

Vol. 74, Iss. 2 — 9 January 1995

Reuse & Permissions
Access Options
Author publication services for translation and copyediting assistance advertisement

Authorization Required


×
×

Images

×

Sign up to receive regular email alerts from Physical Review Letters

Log In

Cancel
×

Search


Article Lookup

Paste a citation or DOI

Enter a citation
×