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

A macromolecular shape function based on sedimentation velocity parameters.

L W Nichol, E A Owen, D J Winzor

    Archives of Biochemistry and Biophysics
    |January 1, 1985
    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

    Insight into the molecular recognition of spermine by DNA quadruplexes from an NMR study of the association of spermine with the thrombin-binding aptamer.

    Journal of molecular recognition : JMR·2013
    Same author

    Fifty years of x-ray production and measurement in medical radiology.

    The British journal of radiology·2010
    Same author

    The effect of temperature on the intensity of X-ray reflexion.

    Proceedings of the Royal Society of London. Series A, Mathematical and physical sciences·2010
    Same author

    Theoretical aspects of the quantitative characterization of ligand binding.

    Current protocols in protein science·2008
    Same author

    On the need to consider kinetic as well as thermodynamic consequences of the parking problem in quantitative studies of nonspecific binding between proteins and linear polymer chains.

    Biophysical chemistry·2006
    Same author

    The development of chromatography for the characterization of protein interactions: a personal perspective.

    Biochemical Society transactions·2003

    A new shape function determined from sedimentation velocity experiments helps elucidate macromolecular geometry. This method provides a simple approach to understanding the shapes of proteins like ovalbumin and myosin.

    Area of Science:

    • Biophysics
    • Physical Chemistry
    • Biochemistry

    Background:

    • Understanding macromolecular geometry is crucial in biophysics.
    • Sedimentation velocity experiments are a key technique for macromolecular characterization.

    Purpose of the Study:

    • To formulate a volume-independent shape function for macromolecules.
    • To relate this function directly to the axial ratio of ellipsoidal macromolecules.
    • To demonstrate its utility in determining macromolecular geometry.

    Main Methods:

    • Formulation of a novel volume-independent shape function.
    • Experimental determination of the shape function using sedimentation velocity experiments.
    • Application of the function to model macromolecules as ellipsoids of revolution.

    Related Experiment Videos

    Main Results:

    • The shape function was successfully formulated and linked to the axial ratio.
    • The method was applied to ovalbumin, bovine serum albumin, and myosin.
    • It offers a straightforward approach for initial geometric elucidation.

    Conclusions:

    • The developed shape function is a valuable tool for macromolecular geometry analysis.
    • Sedimentation velocity experiments provide a practical means to determine this function.
    • This approach simplifies the initial characterization of macromolecular shapes.