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

Muscle proteins--their actions and interactions

K C Holmes1

  • 1Max Planck Institut für medizinische Forschung, Heidelberg, Germany.

Current Opinion in Structural Biology
|December 1, 1996
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

Development of Synchrotron Radiation as a High-Intensity Source for X-ray Diffraction.

Journal of synchrotron radiation·2006
Same author

Introduction.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2005
Same author

The structure of the rigor complex and its implications for the power stroke.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2005
Same author

How X-ray Diffraction with Synchrotron Radiation Got Started.

Journal of synchrotron radiation·2004
Same author

Sir John Cowdery Kendrew.

Biographical memoirs of fellows of the Royal Society. Royal Society (Great Britain)·2004
Same author

Structural mechanism of muscle contraction.

Annual review of biochemistry·2000

Muscle contraction involves myosin cross-bridges rowing actin filaments. Structural studies reveal distinct myosin states and a transformation mechanism, explaining the muscle power stroke.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Muscle contraction is a fundamental biological process driven by the interaction between actin and myosin filaments.
  • Understanding the molecular mechanisms of muscle contraction is crucial for fields ranging from physiology to disease research.

Purpose of the Study:

  • To elucidate the structural details of the myosin motor mechanism during muscle contraction.
  • To characterize the distinct conformational states of myosin S1 and the transformation between them.

Main Methods:

  • Utilized structural studies, including crystallography, to analyze myosin S1 conformations.
  • Investigated the structural basis of the transition between the rigor (down) and products complex (up) states.

Related Experiment Videos

Main Results:

  • Identified distinct structural states for myosin S1: the rigor (ATP-bound, 'down') conformation and the products complex (ADP.Pi, 'up') state.
  • Crystallographic data substantiated this classification and provided details of the conformational transformation.
  • The 'up' to 'down' isomerization, termed the power stroke, involves significant angular changes in the myosin 'lever arm'.

Conclusions:

  • The myosin 'lever arm' rotation during the 'up' to 'down' transition is the primary driver of the muscle power stroke.
  • This structural transformation can account for an 11 nm displacement, explaining the force generation in muscle contraction.