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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...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

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Related Experiment Video

Updated: Jun 12, 2026

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

Deciphering unusually large modulations in two related organic hydroxy channel structures.

Arie van der Lee1, Ioan Stroiu1, Li Bu Huang1

  • 1Institut Européen des Membranes, Université de Montpellier, Montpellier, France.

Acta Crystallographica Section B, Structural Science, Crystal Engineering and Materials
|June 10, 2026
PubMed
Summary

Two organic compounds exhibit pronounced structural modulation due to competing urea-urea and hydroxy-hydroxy interactions. A new graphical method visualizes this modulation, aiding in understanding complex crystal structures.

Keywords:
Lissajous representationmodulated structuremodulation strengthorganic structure

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Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
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Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

Related Experiment Videos

Last Updated: Jun 12, 2026

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

Area of Science:

  • Crystallography
  • Materials Science
  • Organic Chemistry

Background:

  • Incommensurately modulated structures are complex crystal systems.
  • Organic hydroxy-channel compounds can exhibit unique structural properties.
  • Understanding modulation origins is key to predicting material behavior.

Purpose of the Study:

  • To determine and compare the modulated structures of two organic hydroxy-channel compounds.
  • To explore the origin of structural modulation in these compounds.
  • To introduce a novel graphical method for visualizing structural modulation.

Main Methods:

  • X-ray diffraction analysis was used to determine the crystal structures.
  • Comparison of modulated structures with a non-modulated reference compound.
  • Analysis of satellite reflection intensities against a benchmark set of 117 modulated structures.
  • Development of a graphical visualization method using Lissajous curves.

Main Results:

  • The incommensurately modulated structures of two related organic hydroxy-channel compounds were determined.
  • Competition between urea-urea and hydroxy-hydroxy interactions is explored as a potential origin for modulation.
  • The modulation in the studied compounds is unusually pronounced, indicated by strong satellite reflections.
  • A new graphical method effectively visualizes structural modulation within the unit cell.

Conclusions:

  • The study elucidates the pronounced structural modulation in specific organic hydroxy-channel compounds.
  • The findings suggest a competition between intermolecular interactions influences modulation.
  • The introduced graphical method offers an intuitive way to visualize complex structural modulations.