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

Structure and function of myosin filaments.

Roger Craig1, John L Woodhead

  • 1Department of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA. roger.craig@umassmed.edu

Current Opinion in Structural Biology
|March 28, 2006
PubMed
Summary

New imaging techniques reveal the detailed structure of myosin filaments, explaining muscle relaxation at a molecular level. This research clarifies how myosin heads and tails interact to control muscle contraction and cell movement.

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

Thick filament molecular interfaces play a critical role in the pathogenesis of hypertrophic cardiomyopathy.

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

Cryo-EM reveals how cardiomyopathy therapeutic drugs modulate the myosin motors of the heart.

Science advances·2026
Same author

Comparing cryo-EM structures of the vertebrate cardiac muscle thick filament.

Biophysical reviews·2026
Same author

"QuickStainer": a rapid negative staining device for improved preservation of molecular structure.

Journal of structural biology·2026
Same author

Cryo-EM Reveals How Cardiomyopathy Therapeutic Drugs Modulate the Myosin Motors of the Heart.

bioRxiv : the preprint server for biology·2025
Same author

"QuickStainer": a rapid negative staining device for improved preservation of molecular structure.

bioRxiv : the preprint server for biology·2025

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Myosin filaments are crucial for muscle contraction and cell motility, interacting with actin.
  • Previous X-ray and electron microscopy (EM) studies provided general myosin filament organization but lacked detailed descriptions.
  • Technical challenges have historically limited in-depth analysis of myosin structure.

Purpose of the Study:

  • To overcome technical difficulties in visualizing myosin filament organization.
  • To provide detailed insights into the three-dimensional structure of myosin filaments.
  • To elucidate the molecular mechanisms underlying muscle relaxation and myosin regulation.

Main Methods:

  • Advanced ultrastructural and image analysis techniques.

Related Experiment Videos

  • Single-particle three-dimensional (3D) reconstructions.
  • Cryo-electron microscopy (cryo-EM) and crystallographic studies.
  • Atomic structure docking into cryo-EM density maps.
  • Sequence analysis of myosin tails.

    • Main Results:

    • Detailed 3D reconstructions revealed new insights into myosin head and tail organization.
    • Docking atomic structures into cryo-EM maps suggested mechanisms for switching off myosin filaments, leading to muscle relaxation.
    • Sequence analysis indicated probable myosin tail interactions within the filament backbone.
    • Direct visualization of tail interactions in 3D is emerging from crystallographic and EM studies.

    Conclusions:

    • Improved imaging techniques are enabling detailed structural descriptions of myosin filaments.
    • Understanding myosin organization provides insights into the regulation of muscle contraction and relaxation.
    • The research clarifies how myosin filaments are switched off, contributing to the understanding of muscle relaxation.