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

The structure of oriented sphingomyelin bilayers

R S Khare, C R Worthington

    Biochimica Et Biophysica Acta
    |December 19, 1978
    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

    X-RAY STUDIES ON NERVE AND PHOTORECEPTORS.

    Annals of the New York Academy of Sciences·2017
    Same author

    Along the road not taken: how many myosin heads act on a single actin filament at any instant in working muscle?

    Progress in biophysics and molecular biology·2011
    Same author

    The diffuse scattering problem in membrane diffraction: a solution.

    Biophysical journal·2009
    Same author

    Muscle contraction: a new interpretation of the transient behaviour of muscle.

    International journal of biological macromolecules·2005
    Same author

    Muscle contraction: energy rate equations in relation to efficiency and step-size distance.

    International journal of biological macromolecules·2003
    Same author

    Muscle contraction: viscous-like frictional forces and the impulsive model.

    International journal of biological macromolecules·2001

    X-ray diffraction reveals sphingomyelin bilayers maintain a stable lamellar repeat of 68.5 A, irrespective of humidity. Molecular models suggest a structure similar to other phospholipids, with head groups aligned parallel to the membrane.

    Area of Science:

    • Biophysics
    • Materials Science
    • Structural Biology

    Background:

    • Sphingomyelin is a crucial component of biological membranes.
    • Understanding its bilayer structure is key to membrane function.

    Purpose of the Study:

    • To elucidate the molecular structure of sphingomyelin in oriented bilayers.
    • To compare sphingomyelin's structure with other phospholipids.

    Main Methods:

    • X-ray diffraction analysis of oriented sphingomyelin bilayers.
    • Low-resolution X-ray data deconvolution.
    • Patterson function comparison with phosphatidylcholine and phosphatidylethanolamine.
    • Molecular model calculations.
    • Electron density profile generation.

    Related Experiment Videos

    Main Results:

    • Observed a lamellar repeat of 68.5 A and equatorial reflections (strong 4.2 A) in sphingomyelin bilayers.
    • Diffraction spacings remained constant across varying humidities.
    • Electron density profiles at ~6 A and ~2.5 A resolution were obtained.
    • Sphingomyelin structure resembles phosphatidylcholine and phosphatidylethanolamine.

    Conclusions:

    • Sphingomyelin's phosphorylcholine head group lies in the membrane plane, perpendicular to hydrocarbon chains.
    • Hydrocarbon chains are nearly parallel, with minimal interdigitation between adjacent molecules.