Related Experiment Video

Updated: Aug 19, 2026

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
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Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

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Force-velocity relationships in kinesin-driven motility

K Hall1, D G Cole, Y Yeh

  • 1Section of Molecular and Cellular Biology, University of California, Davis 95616.

Nature
|July 29, 1993
PubMed

Insights

Kinesin motor proteins move cellular components along microtubules. Using a centrifuge microscope, researchers measured kinesin

Area of Science:

  • Cell biology
  • Biophysics
  • Molecular motors

Background:

  • Kinesin is a microtubule-based motor protein essential for intracellular transport.
  • It utilizes Mg-ATP hydrolysis to generate force, moving cargo towards microtubule plus ends.
  • Existing methods for studying kinesin motility have limitations in force generation analysis.

Purpose of the Study:

  • To investigate the force-velocity relationship of kinesin-driven motility.
  • To quantify the maximal isometric force generated by individual kinesin molecules.

Main Methods:

  • Utilized a centrifuge microscope for high-resolution motility assays.
  • Obtained force-velocity curves for kinesin-driven microtubule movement.
  • Calculated the maximal isometric force per kinesin molecule.

Main Results:

  • Successfully generated force-velocity curves for kinesin motility.
  • Estimated the maximal isometric force per kinesin molecule to be 0.12 ± 0.03 pN.

Conclusions:

  • The centrifuge microscope is a valuable tool for quantifying kinesin force generation.
  • Provides a precise measurement of the force output of single kinesin motors.

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