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

Ionic channels with conformational substates.

P Läuger

    Biophysical Journal
    |May 1, 1985
    PubMed
    Summary

    Ionic channels exhibit dynamic conformational substates that influence their function. These hidden states can alter channel properties like conductance and ion flux, impacting biological processes.

    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

    Orientation of the porphyrin ring in artificial chlorophyll membranes.

    The Journal of membrane biology·2013
    Same author

    Transport mechanism of hydrophobic ions through lipid bilayer membranes.

    The Journal of membrane biology·2013
    Same author

    Space charge-limited conductance in lipid bilayer membranes.

    The Journal of membrane biology·2013
    Same author

    Interaction of cytochromec with phospholipid monolayers and bilayer membranes.

    The Journal of membrane biology·2013
    Same author

    Optical properties of artificial chlorophyll membranes.

    The Journal of membrane biology·2013
    Same author

    Charge translocation by the Na,K-pump: I. Kinetics of local field changes studied by time-resolved fluorescence measurements.

    The Journal of membrane biology·1991

    Area of Science:

    • Biophysics
    • Molecular Biology
    • Ion Channel Physiology

    Background:

    • Protein dynamics indicate ionic channels possess multiple conformational substates.
    • Long-lived substates are observable, but many are too transient for current experimental resolution.
    • These 'hidden' substates can significantly affect measurable channel properties.

    Purpose of the Study:

    • To explore the functional implications of transient conformational substates in ionic channels.
    • To investigate how these substates influence channel conductance, rectification, and ion flux coupling.
    • To examine the impact of ion binding on conformational transition rates and microscopic reversibility.

    Main Methods:

    • Theoretical analysis of protein dynamics and ionic channel function.
    • Modeling of conformational substates and their effect on single-channel currents.
    • Examination of ion-protein interactions and their influence on transition kinetics.

    Main Results:

    • Hidden substates can alter concentration-dependent conductance and create intrinsic rectification.
    • Coupling of ionic fluxes can occur even with single binding sites due to conformational changes.
    • Ion binding can modulate transition rates, leading to non-equilibrium distributions and apparent violations of microscopic reversibility.

    Conclusions:

    • Transient conformational substates are critical determinants of ionic channel behavior.
    • Understanding these dynamics is essential for interpreting channel function and developing new therapeutic strategies.
    • The interplay between ion occupancy and protein conformation challenges traditional models of channel kinetics.

    Related Experiment Videos