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Related Concept Videos

Non-gated Ion Channels01:24

Non-gated Ion Channels

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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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Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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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 Channels01:19

Ligand-gated Ion Channels

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Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
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Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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

Ligand-Gated Ion Channel Receptor: Gating Mechanism

4.1K
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...
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G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
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Fabrication and Characterization of Superconducting Resonators
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Multi-Valley Superconductivity in Ion-Gated MoS2 Layers.

Erik Piatti1, Domenico De Fazio2, Dario Daghero1

  • 1Department of Applied Science and Technology , Politecnico di Torino , 10129 Torino , Italy.

Nano Letters
|June 28, 2018
PubMed
Summary

Superconductivity in molybdenum disulfide (MoS2) emerges when multiple electron pockets in its Fermi surface become populated, not just two. This multivalley Fermi surface topology is crucial for the superconducting state onset.

Keywords:
Lifshitz transitionsRaman spectroscopyTransition metal dichalcogenideselectron−phonon couplingionic gatingsuperconductivity

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Area of Science:

  • Condensed Matter Physics
  • Materials Science
  • Quantum Phenomena

Background:

  • Transition metal dichalcogenides (TMDs) exhibit unique electronic properties in 2D, including field-tunable phase transitions.
  • Semiconducting TMDs like MoS2 can achieve surface superconductivity (SC) via electrostatic doping, but the underlying mechanism remains under investigation.

Purpose of the Study:

  • To investigate the role of Fermi surface (FS) topology in the electrostatic doping-induced superconductivity of MoS2.
  • To determine the relationship between electron pocket population and the onset of the superconducting state in MoS2.

Main Methods:

  • Low-temperature electrical transport measurements were conducted on ion-gated MoS2 flakes.
  • Systematic variation of electrostatic doping concentration to probe changes in electronic structure and superconductivity.

Main Results:

  • A fully multivalley Fermi surface (FS) is experimentally confirmed to be associated with the onset of superconductivity in MoS2.
  • The Q/Q' valleys of the FS populate at doping levels exceeding 2 × 10^13 cm^-2.
  • Superconductivity emerges only after the Fermi level crosses both spin-orbit split sub-bands (Q1 and Q2), indicating a Lifshitz transition.

Conclusions:

  • The superconducting state in MoS2 is intrinsically linked to the connectivity and topology of its multivalley Fermi surface.
  • Simultaneous population of multiple electron pockets, driven by a Lifshitz transition, promotes superconductivity.
  • The identified FS topology provides a critical guideline for discovering new superconductors in 2D materials.