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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...
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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...
Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: May 17, 2026

Determination of the Photoisomerization Quantum Yield of a Hydrazone Photoswitch
09:33

Determination of the Photoisomerization Quantum Yield of a Hydrazone Photoswitch

Published on: February 7, 2022

Isoindolinone-based molecular switches.

Michael Lawson1, Sara Eisler

  • 1Department of Chemistry, University of New Brunswick, Fredericton, NB, Canada.

Organic & Biomolecular Chemistry
|October 17, 2012
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel multi-stable molecular switch. This switch exhibits three stable states, with two states reversibly controlled by light or acid, advancing molecular control technologies.

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Area of Science:

  • Molecular engineering
  • Organic chemistry
  • Supramolecular chemistry

Background:

  • Molecular switches are crucial for controlling molecular conformation and function.
  • Bistable molecular switches are common, but multi-stable switches are rare.
  • Controlling molecular states is essential for advanced materials and devices.

Purpose of the Study:

  • To introduce a new class of molecular switches with multiple stable states.
  • To demonstrate reversible control over molecular conformations using external stimuli.
  • To explore the potential of multi-stable switches in molecular engineering.

Main Methods:

  • Synthesis of a novel molecular architecture designed for multi-stability.
  • Characterization of distinct molecular conformations using spectroscopic and crystallographic techniques.
  • Investigation of stimuli-responsive behavior using light and acid as external triggers.

Main Results:

  • A new class of molecular switch capable of forming three stable states was synthesized.
  • Two of the stable states were shown to interconvert reversibly.
  • Light and acid were identified as effective triggers for reversible state switching.

Conclusions:

  • The developed molecular switch offers unprecedented multi-stability and external control.
  • This work expands the toolkit for designing sophisticated molecular machines.
  • The findings pave the way for new applications in responsive materials and molecular devices.