Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Measuring kinesin's first step.

Steven S Rosenfeld1, Jun Xing, Geraldine M Jefferson

  • 1Department of Neurology, University of Alabama at Birmingham and Neurology Service, Department of Veterans Affairs Medical Center, Birmingham, Alabama 35294, USA. stevensr@uab.edu

The Journal of Biological Chemistry
|July 18, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Effect of Low-Dose Estradiol on the Clinical Pregnancy Rate of the Hormone Replacement Frozen-Thawed Embryo Transfer Cycle.

International journal of women's health·2026
Same author

Multi-sampling allows intra-tumoral heterogeneity querying and vulnerability profiling in glioblastoma.

Neuro-oncology·2026
Same author

From Nutritional Profile to Circular Bioeconomy: A Review of Sea Buckthorn Oil and By-Product Valorization.

Foods (Basel, Switzerland)·2026
Same author

Enamel proteins from six Homo erectus specimens across China.

Nature·2026
Same author

Rethinking the role of synergy calculations in the next century of drug combination discovery.

Med (New York, N.Y.)·2026
Same author

Monoclonal antibodies against nitrated nerve growth factor reveal an oxidation-dependent pathogenic hallmark in ALS.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
Same journal

PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

The Journal of biological chemistry·2026
See all related articles

New spectroscopic probes reveal how the molecular motor kinesin moves. This research measures kinesin

Area of Science:

  • Molecular Biology
  • Biophysics
  • Cellular Motor Proteins

Background:

  • Kinesin is a molecular motor essential for intracellular transport, moving cargo along microtubules.
  • Existing models propose kinesin's catalytic domains separate during its 8-nm step cycle, with ATP hydrolysis powering movement.
  • The precise timing of ATP hydrolysis and product release relative to kinesin's stepping, and the kinetics of domain separation and microtubule binding, remain unquantified.

Purpose of the Study:

  • To develop novel spectroscopic probes to investigate kinesin's processive movement mechanism.
  • To directly measure the kinetics of kinesin's stepping, microtubule binding, and domain separation.
  • To provide critical data for evaluating competing models of kinesin function.

Main Methods:

Related Experiment Videos

  • Development of spectroscopic probes with fluorescence sensitive to motor-motor separation and microtubule binding.
  • Utilizing fluorescence kinetics to monitor and quantify the dynamic interactions of kinesin during its motor activity.
  • Direct measurement of the rates of kinesin stepping onto and releasing from microtubules.

    • Main Results:

    • Successfully developed spectroscopic probes to monitor kinesin-kinesin separation and microtubule binding.
    • Kinetics of fluorescence changes allowed direct measurement of kinesin's stepping and release rates.
    • Provided new insights into the temporal relationship between ATP hydrolysis, product release, and motor stepping.

    Conclusions:

    • The developed spectroscopic methods enable direct kinetic measurements of kinesin motor function.
    • These measurements offer crucial data to differentiate between existing models of kinesin processivity.
    • Understanding kinesin's precise stepping and binding kinetics is key to elucidating how sustained processive movement is achieved.