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Related Concept Videos

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...
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...
Ion Channels01:19

Ion Channels

The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow specific...
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.

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Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

Synthetic ion channels: functional analysis and structural studies.

Ulrich Koert1

  • 1Fachbereich Chemie, Philipps-Universität Marburg, D-35032 Marburg, Germany. koert@chemie.uni-marburg.de

Physical Chemistry Chemical Physics : PCCP
|October 1, 2009
PubMed
Summary
This summary is machine-generated.

Researchers created synthetic ion channels inspired by gramicidin A. These channels show selective ion transport and conformational changes, offering insights into membrane interactions and channel design.

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Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
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Area of Science:

  • Biophysical Chemistry
  • Molecular Biophysics
  • Synthetic Biology

Background:

  • Gramicidin A serves as a structural template for synthetic ion channel design.
  • Understanding ion transport mechanisms in biological and synthetic channels is crucial for various applications.
  • Lipid bilayer interactions and channel conformational dynamics influence ion permeation.

Purpose of the Study:

  • To engineer and characterize synthetic ion channels based on the gramicidin A beta-helix structure.
  • To investigate ion transport properties, including selectivity and efficiency, through these synthetic channels.
  • To explore the relationship between channel structure, membrane environment, and ion-induced conformational changes.

Main Methods:

  • Single-channel current measurements in planar lipid bilayers.
  • Synthesis of gramicidin A analogs, including THF-gramicidin hybrids and minigramicidins.
  • Dwell-time analysis to study hydrophobic coupling with lipid bilayers of varying thickness.
  • Investigation of ion-induced conformational changes using spectroscopic or electrophysiological techniques.

Main Results:

  • Synthetic ion channels derived from gramicidin A were successfully constructed.
  • Asymmetric THF-gramicidin hybrids demonstrated selective insertion into phospholipid bilayers.
  • Ion selectivity was achieved using synthetic cyclohexyl-ether amino acids as building blocks.
  • Minigramicidins exhibited hydrophobic coupling with membranes, and Cs(+)-ion addition induced a beta-helix conformational switch.

Conclusions:

  • Synthetic ion channels can be rationally designed to mimic natural channel functions.
  • Tailoring channel building blocks and structure allows for control over ion selectivity and membrane interactions.
  • Ion-binding events can trigger significant conformational changes in synthetic channels, impacting their function.