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

Conformational changes induced by ionic strength and pH in two bovine myelin basic proteins.

W H Thomas, U Weser, K Hempel

    Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
    |October 1, 1977
    PubMed
    Summary

    Myelin proteins A1 and P2 exhibit distinct structural stability and conformational changes in response to pH and urea. These differences in myelin protein structure may correlate with their biological functions.

    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

    Variability of non-clinical behavioral CNS safety assessment: An intercompany comparison.

    Journal of pharmacological and toxicological methods·2019
    Same author

    Dropped-head syndrome in a patient under treatment with the MEK inhibitor trametinib for NRAS-mutated metastatic melanoma.

    Clinical and experimental dermatology·2017
    Same author

    Activity of Cu2Zn2 superoxide dismutase against the human immunodeficiency virus type 1.

    Redox report : communications in free radical research·2016
    Same author

    COMPARISON OF HALF-SATURATION CONSTANTS FOR GROWTH AND NITRATE UPTAKE OF MARINE PHYTOPLANKTON (2).

    Journal of phycology·2016
    Same author

    EFFECTS OF TEMPERATURE AND ILLUMINANCE ON CELL DIVISION RATES OF THREE SPECIES OF TROPICAL OCEANIC PHYTOPLANKTON(1).

    Journal of phycology·2016
    Same author

    Solubility behavior of three aromatic hydrocarbons in distilled water and natural seawater.

    Environmental science & technology·2012

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Structural Biology

    Background:

    • Myelin proteins are crucial for nerve insulation in both central and peripheral nervous systems.
    • Understanding the structural properties of myelin proteins like A1 and P2 is key to comprehending their biological roles.

    Purpose of the Study:

    • To investigate and compare the structural stability and conformational behavior of myelin proteins A1 and P2.
    • To explore potential structure-function relationships based on observed differences.

    Main Methods:

    • Proteins A1 (central nervous system) and P2 (peripheral nervous system) were isolated from nerve tissues.
    • Circular dichroism spectroscopy was employed to examine conformational changes in aqueous solutions across varying pH and urea concentrations.

    Related Experiment Videos

    Main Results:

    • Both A1 and P2 proteins demonstrated stable secondary structures between pH 2.5 and 11.7.
    • A1 protein remained stable up to pH 13, unlike P2 protein.
    • Differential stereochemical responses to urea were observed: A1 showed a linear change, while P2 exhibited a sigmoidal curve.

    Conclusions:

    • Myelin proteins A1 and P2 possess distinct structural characteristics and stabilities.
    • The observed differences in conformational changes, particularly in the presence of urea, suggest unique structural properties for each protein.
    • These findings support the potential for correlations between the structure and function of basic myelin proteins.