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 Concept Videos

Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential.
Electrochemical Gradient and Channel Proteins: An Overview01:21

Electrochemical Gradient and Channel Proteins: An Overview

An electrochemical gradient is a fundamental concept in biology and chemistry. It regulates the movement of ions across cell membranes. This movement is influenced by two factors:
The electrical gradient: The electrical gradient across cell membranes refers to the difference in electric charge between the inside and outside of a cell.  This difference drives the movement of ions towards or away from the cells. For instance, if the inside of the cell is more negatively charged relative to the...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Enhancing Relative Binding Free Energy Calculation with Grand Canonical Monte Carlo, Water-swap Monte Carlo, Terminal-flip Monte Carlo and Replica Exchange Solute Tempering.

Journal of chemical theory and computation·2026
Same author

Hydrophobic and lipid-mediated gating mechanism revealed by low-conductance MthK mutants.

bioRxiv : the preprint server for biology·2026
Same author

Collecting Large Datasets of Unambiguous Structural Restraints for Protein Structure Determination by 4D Proton-Detected Solid-State NMR.

Chemphyschem : a European journal of chemical physics and physical chemistry·2026
Same author

Targeting the Membrane-Embedded Rhomboid Protease GlpG: A Multimodal Strategy for Inhibitor Discovery and Mechanistic Insight.

Angewandte Chemie (International ed. in English)·2026
Same author

One pocket to activate them all (?): Efforts on understanding the modulator pocket in K2P channels.

Channels (Austin, Tex.)·2025
Same author

Structural insights into AQP3 channel closure upon pH and redox changes reveal an autoregulatory molecular mechanism.

Nature communications·2025

Related Experiment Video

Updated: Jun 6, 2026

Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

Functional dynamics in the voltage-dependent anion channel.

Saskia Villinger1, Rodolfo Briones, Karin Giller

  • 1Department of NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|December 15, 2010
PubMed
Summary

The voltage-dependent anion channel (VDAC1) exhibits increased N-terminal dynamics, crucial for its function. A specific glutamic acid (E73) is key to these dynamics and VDAC1 gating, impacting metabolite transport and apoptosis.

More Related Videos

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

Published on: June 2, 2023

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

Related Experiment Videos

Last Updated: Jun 6, 2026

Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

Published on: June 2, 2023

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • The voltage-dependent anion channel (VDAC) is a critical gatekeeper in the outer mitochondrial membrane, regulating metabolite transport.
  • VDAC1, a major isoform, plays a role in cellular metabolism and apoptosis.
  • Understanding VDAC1's dynamic behavior is essential for elucidating its gating mechanisms.

Purpose of the Study:

  • To investigate the functional dynamics of VDAC1.
  • To identify key residues and regions involved in VDAC1's dynamic properties.
  • To correlate VDAC1 dynamics with its interaction and gating functions.

Main Methods:

  • Solution NMR spectroscopy
  • Gaussian network model analysis
  • Molecular dynamics simulations
  • Site-directed mutagenesis

Main Results:

  • Micro- to millisecond dynamics were significantly increased in the N-terminal six β-strands of VDAC1 in micellar solution.
  • Molecular dynamics simulations identified glutamic acid 73 (E73) as a key residue influencing N-terminal dynamics and membrane thinning.
  • Mutation or modification of E73 substantially reduced these dynamics.
  • E73 is essential for hexokinase-I-induced VDAC channel closure and apoptosis inhibition.

Conclusions:

  • Micro- to millisecond dynamics in VDAC1's N-terminal region are vital for its interaction with other proteins and channel gating.
  • The charge on E73 is a critical determinant of VDAC1's dynamic behavior and functional regulation.
  • These findings provide insights into the molecular mechanisms underlying VDAC1-mediated metabolite transport and apoptosis control.