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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...

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High-Sensitivity Nuclear Magnetic Resonance at Giga-Pascal Pressures: A New Tool for Probing Electronic and Chemical Properties of Condensed Matter under Extreme Conditions
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Flying-patch patch-clamp study of G22E-MscL mutant under high hydrostatic pressure.

Evgeny Petrov1, Paul R Rohde, Boris Martinac

  • 1Victor Chang Cardiac Research Institute, Darlinghurst, Australia. petrov67@gmail.com

Biophysical Journal
|April 6, 2011
PubMed
Summary

High hydrostatic pressure (HHP) surprisingly increases the opening probability of the G22E-MscL mechanosensitive channel. This pressure effect, observed up to 90 MPa, offers new insights into complex channel gating mechanisms.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Physiology

Background:

  • High hydrostatic pressure (HHP) significantly influences cellular structures and protein functions.
  • Mechanosensitive channels, like E. coli MscL, are crucial for cellular response to mechanical stress.

Purpose of the Study:

  • To investigate the impact of HHP on the G22E-MscL mutant, a constitutively open bacterial mechanosensitive channel.
  • To explore pressure-induced alterations in channel gating kinetics and open probability.

Main Methods:

  • Utilized the patch-clamp technique with a flying-patch device and hydraulic setup.
  • Studied the G22E-MscL channel reconstituted in liposomes and expressed in E. coli giant spheroplasts.
  • Applied pressures ranging from 0.1 MPa to 90 MPa.

Main Results:

  • Contrary to thermodynamic expectations, HHP (0.1-90 MPa) increased the open probability of the G22E-MscL channel.
  • Observed pressure-dependent alterations in channel kinetics, including gating at subconducting levels.
  • Proposed that water molecule hydration of the hydrophobic gate under HHP facilitates channel opening.

Conclusions:

  • HHP can enhance the open state of the G22E-MscL channel, even without membrane tension.
  • HHP serves as a valuable tool for elucidating the gating mechanisms of complex ion channels like MscL.
  • Findings challenge traditional thermodynamic predictions regarding pressure effects on channel function.