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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...
Non-gated Ion Channels01:24

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.
Non-gated Ion Channels01:24

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.
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...

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Related Experiment Video

Updated: May 30, 2026

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
11:42

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

Published on: January 22, 2015

Coarse grained model for exploring voltage dependent ion channels.

Anatoly Dryga1, Suman Chakrabarty, Spyridon Vicatos

  • 1Department of Chemistry, University of Southern California, Los Angeles, CA 90089-1062, USA.

Biochimica Et Biophysica Acta
|August 17, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a coarse-grained model for simulating voltage-activated ion channels under external potentials. The model accurately describes electrolyte behavior and protein interactions, offering insights into channel gating mechanisms.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Electrochemistry

Background:

  • Simulating external voltage effects on membrane proteins is challenging due to limitations in current molecular and macroscopic models.
  • Understanding voltage-gated ion channels requires accurate modeling of membrane potential and electrolyte interactions.

Purpose of the Study:

  • To extend a coarse-grained (CG) model for simulating membrane/protein systems under external electric potentials.
  • To develop a consistent method for modeling electrode-electrolyte-protein interactions in voltage-activated systems.
  • To provide a link between microscopic and macroscopic descriptions of electrolyte behavior.

Main Methods:

  • Developed an extended coarse-grained model incorporating semimacroscopic electrolyte descriptions.
  • Coupled electrode potentials, electrolyte behavior, and protein ionization.
  • Validated the model against established theories (Debye-Huckel, Gouy-Chapman) and electrode systems.
  • Applied the model to study gating charge in the Kv1.2 channel.

Main Results:

  • The model provides a clear description of charge distribution in electrolyte systems, including near electrodes.
  • It offers insights into electrolyte charge distribution changes during membrane equilibration and gating.
  • Preliminary results for the Kv1.2 channel reveal gating charge based on electrolyte charge distribution shifts.
  • The model captures changes in protein residue protonation states during voltage-induced transitions.

Conclusions:

  • The extended CG model offers a powerful tool for studying voltage-activated channels by balancing protein conformational energy and external potential interactions.
  • This approach provides a more accurate representation of gating charge and associated phenomena compared to conventional methods.
  • The model's ability to capture protonation state changes enhances its utility for understanding channel function.