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

Single-channel acetylcholine receptor kinetics.

M D Leibowitz, V E Dionne

    Biophysical Journal
    |January 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Researchers developed single-channel ensemble analysis to study acetylcholine receptor activation. This method estimates kinetic rates of channel opening and closing, revealing voltage and agonist dependencies.

    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

    Limulus Retinal mRNA Induces Light-Dependent Currents in Xenopus Oocytes.

    The Biological bulletin·2017
    Same author

    Design and synthesis of benzofused heterocyclic RXR modulators.

    Bioorganic & medicinal chemistry letters·2004
    Same author

    Design and synthesis of fluorinated RXR modulators.

    Bioorganic & medicinal chemistry letters·2003
    Same author

    Novel (2E,4E,6Z)-7-(2-alkoxy-3,5-dialkylbenzene)-3-methylocta-2,4,6-trienoic acid retinoid X receptor modulators are active in models of type 2 diabetes.

    Journal of medicinal chemistry·2003
    Same author

    Attenuation of colon inflammation through activators of the retinoid X receptor (RXR)/peroxisome proliferator-activated receptor gamma (PPARgamma) heterodimer. A basis for new therapeutic strategies.

    The Journal of experimental medicine·2001
    Same author

    Differential effects of rexinoids and thiazolidinediones on metabolic gene expression in diabetic rodents.

    Molecular pharmacology·2001
    Same journal

    Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

    Biophysical journal·2026
    Same journal

    Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

    Biophysical journal·2026
    Same journal

    Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.

    Biophysical journal·2026
    Same journal

    Dynamic conformations of fluorophores on self-labeling protein tags.

    Biophysical journal·2026
    Same journal

    Different actions of RyR2 open and closed channel block explained by a multiscale Ca<sup>2+</sup> release model.

    Biophysical journal·2026
    Same journal

    Membrane Environment Sets the Functional pK<sub>a</sub> of Ionizable Lipids.

    Biophysical journal·2026
    See all related articles

    Area of Science:

    • Neuroscience
    • Biophysics
    • Molecular Biology

    Background:

    • Junctional acetylcholine receptors (AChRs) mediate fast synaptic transmission.
    • Understanding AChR activation mechanisms is crucial for neuromuscular function.

    Purpose of the Study:

    • To develop and validate a novel analytical approach for estimating kinetic transition rates of AChR channel activation.
    • To investigate the voltage and agonist dependencies of these kinetic rates.

    Main Methods:

    • Single-channel ensemble analysis was developed to estimate kinetic transition rate constants.
    • The method was validated using simulated single-channel data.
    • Experimental data from acetylcholine-activated single channels at the garter snake neuromuscular junction were analyzed.

    Related Experiment Videos

    Main Results:

    • Estimated rate constants for opening, closing, and leaving the doubly-liganded closed state were determined.
    • All three rate constants exhibited voltage dependence.
    • The channel-closing rate was found to be agonist-dependent, differing between carbamylcholine and acetylcholine.

    Conclusions:

    • Single-channel ensemble analysis provides a robust method for probing AChR gating kinetics.
    • Kinetic rates of AChR activation are significantly influenced by membrane potential and agonist identity.
    • This approach offers insights into the molecular mechanisms underlying synaptic transmission.