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

Myosin flexibility: structural domains and collective vibrations.

Isabelle Navizet1, Richard Lavery, Robert L Jernigan

  • 1Molecular Structure Section, Laboratory of Experimental and Computational Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5677, USA.

Proteins
|January 30, 2004
PubMed
Summary

Myosin motor movement relies on conformational changes. This study used structural data and elastic network models to reveal conserved domains and myosin flexibility, highlighting the role of light chains and nucleotide binding.

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

Proteome-wide analysis of protein stability in Escherichia coli under acid stress.

Journal of industrial microbiology & biotechnology·2026
Same author

Simulating Steady-State Spectra of Acrolein while Accounting for Nuclear Quantum Effects.

The journal of physical chemistry. A·2026
Same author

PET-FBA: A lightweight enzyme allocation and thermodynamics-constrained flux analysis approach to explore Escherichia coli metabolic adaptation to intracellular acidification.

Metabolic engineering·2025
Same author

Large Numbers of New Human Paralogs Discovered.

bioRxiv : the preprint server for biology·2025
Same author

Porphyrin-Based Bio-Sourced Materials for Water Depollution Under Light Exposure.

Polymers·2025
Same author

Chemiluminescent 2-Coumaranones: Synthesis, Luminescence Mechanism, and Emerging Applications.

Molecules (Basel, Switzerland)·2025

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Myosin motor protein movement along actin filaments is crucial for cellular functions.
  • This movement involves conformational changes in the myosin cross-bridge.
  • The precise mechanics of these conformational changes remain poorly understood.

Purpose of the Study:

  • To investigate the mechanics of myosin conformational changes using structural and computational methods.
  • To identify structurally conserved domains within the myosin motor protein.
  • To elucidate the factors influencing myosin flexibility, including light chains and nucleotide binding.

Main Methods:

  • Utilized existing crystallographic structures of three myosin head conformations.
  • Performed structural comparisons of different myosin states.

Related Experiment Videos

  • Employed a coarse-grained elastic network model for mechanical studies.

    • Main Results:

    • Defined structurally conserved domains within the myosin motor protein.
    • Gained a better understanding of myosin flexibility.
    • Identified a rigidifying role for light chains in the myosin lever arm.
    • Observed changes in myosin flexibility correlated with nucleotide binding.

    Conclusions:

    • The study provides structural insights into the mechanical basis of myosin motor function.
    • Myosin flexibility is modulated by light chains and nucleotide interactions.
    • These findings contribute to a deeper understanding of muscle contraction and molecular motor mechanisms.