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

Human spectrin. VI. A viscometric study

B T Stokke, A Elgsaeter

    Biochimica Et Biophysica Acta
    |February 6, 1981
    PubMed
    Summary
    This summary is machine-generated.

    Human spectrin heterodimers and heterotetramers flexibility was studied using viscometry. Results show spectrin

    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

    Improved chitosan-mediated gene delivery based on easily dissociated chitosan polyplexes of highly defined chitosan oligomers.

    Gene therapy·2004
    Same author

    Macromolecular triplex zipping observed in derivatives of fungal (1 --> 3)-beta-D-glucan by electron and atomic force microscopy.

    Biopolymers·2001
    Same author

    The cytokine stimulating activity of (1-->3)-beta-D-glucans is dependent on the triple helix conformation.

    Carbohydrate research·2000
    Same author

    Deconvolution can be used in electrooptic studies to correct for non-ideal electric excitation pulses only when the electric dipole moment of the studied molecules is predominantly induced.

    Journal of biochemical and biophysical methods·2000
    Same author

    Transient electric birefringence of human erythroid spectrin dimers and tetramers at ionic strengths of 4 mM and 53 mM.

    European biophysics journal : EBJ·1999
    Same author

    The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism.

    The Journal of biological chemistry·1999
    Same journal

    Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Molecular Basis of Disease Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    General Subjects Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

    Biochimica et biophysica acta·2019
    Same journal

    Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

    Biochimica et biophysica acta·2019
    Same journal

    Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

    Biochimica et biophysica acta·2019
    See all related articles

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Biophysics

    Background:

    • Spectrin is a crucial protein in the erythrocyte cytoskeleton.
    • Understanding spectrin's structural properties is vital for cell membrane stability.

    Purpose of the Study:

    • To investigate the molecular flexibility of human spectrin heterodimers and heterotetramers.
    • To determine the impact of ionic strength on spectrin's hydrodynamic properties.

    Main Methods:

    • Viscometry was employed to measure intrinsic viscosity.
    • Experiments were conducted in aqueous solutions with varying salt concentrations.

    Main Results:

    • Intrinsic viscosity of spectrin heterodimers and heterotetramers was determined at 0.1 M NaCl.

    Related Experiment Videos

  • Viscosity significantly increased as ionic strength decreased to 2 mM.
  • Calculated contour lengths suggest flexible spectrin molecules (110 nm for heterodimers, 200 nm for heterotetramers).

    • Conclusions:

    • Human spectrin heterodimers and heterotetramers exhibit significant molecular flexibility.
    • Ionic strength plays a critical role in modulating spectrin's solution behavior.
    • The findings provide insights into spectrin's structural dynamics and mechanical properties.