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Related Concept Videos

Patch Clamp01:18

Patch Clamp

Many fundamental cell functions such as muscle contraction and nerve transmission rely on the electrical signals produced by the movement of positively and negatively charged ions across the cell membrane. One competent method to record current flowing across the whole cell or single ion channel is the patch-clamp technique.
In this method, a glass micropipette containing electrolyte solution is tightly sealed against a small portion of the cell membrane. As a result, a patch of the cell...
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...

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Related Experiment Video

Updated: Jun 4, 2026

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

State-dependent cAMP binding to functioning HCN channels studied by patch-clamp fluorometry.

Shengjun Wu1, Zhanna V Vysotskaya, Xinping Xu

  • 1Department of Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, Virginia, USA.

Biophysical Journal
|March 1, 2011
PubMed
Summary
This summary is machine-generated.

Researchers studied cyclic adenosine monophosphate (cAMP) binding and gating in HCN channels. They found ligand binding changes correlate with channel opening, but unbinding is slower than closing, revealing insights into allosteric regulation.

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Last Updated: Jun 4, 2026

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Published on: March 11, 2021

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Area of Science:

  • Molecular and Cellular Biology
  • Biophysics
  • Neuroscience

Background:

  • Understanding ion channel gating mechanisms is crucial for deciphering cellular signaling.
  • Distinguishing ligand binding from channel gating in ligand-gated channels remains a challenge.

Purpose of the Study:

  • To investigate the relationship between ligand binding and gating in hyperpolarization-activated cyclic nucleotide-gated (HCN) channels.
  • To explore the molecular events underlying cyclic adenosine monophosphate (cAMP)-dependent channel activation.

Main Methods:

  • Utilized patch-clamp fluorometry with a novel fluorescent cAMP analog.
  • Simultaneously recorded HCN channel opening and cAMP binding.
  • Investigated ligand binding affinities in different channel states.

Main Results:

  • Observed a significant increase in cAMP binding upon channel activation, supporting allosteric models.
  • Ligand binding kinetics closely mirrored channel activation kinetics.
  • Identified a slower ligand unbinding rate compared to channel closing during deactivation.

Conclusions:

  • Protein allostery can be achieved by differential ligand binding affinities in resting and active states.
  • HCN channel gating exhibits a delayed response in ligand unbinding relative to membrane potential changes.
  • Provides novel insights into cAMP-dependent gating and allosteric regulation in ligand-gated channels.