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Minimal viral K plus channels as robust model systems for understanding structure/function correlations

Braun, Christian and Schroeder, Indra and Henkes, Leonhard M. and Arrigoni, Cristina and Kast, Stefan M. and Moroni, Anna and Thiel, Gerhard (2013):
Minimal viral K plus channels as robust model systems for understanding structure/function correlations.
In: European biophysics journal : EBJ, pp. S79, 42, (Suppl. 1), ISSN 0175-7571,
[Article]

Abstract

The channel proteins from Chlorella viruses are miniature versions of K+ channels; in essence they represent the pore module of complex K+ channels from eukaryotes. The combination of small size and robust function makes them good model systems for understanding basic structure/function correlates in K+ channels. The channel Kcv NTS counts only 82 amino acids per monomer and molecular dynamics simulations suggest that the channel is quasi fully embedded in the membrane bilayer. The intimate interaction between the channel protein and the surrounding bilayer offers the possibility to examine the performance of the channel in different experimental systems. We therefore performed single channel experiments in vertical and horizontal lipid bilayers as well in the membrane of native HEK-cellsystem. Furthermore we monitored channel conductance and gating in lipids with different head-groups and/or lipids with fatty acid chains of different length.

Item Type: Article
Erschienen: 2013
Creators: Braun, Christian and Schroeder, Indra and Henkes, Leonhard M. and Arrigoni, Cristina and Kast, Stefan M. and Moroni, Anna and Thiel, Gerhard
Title: Minimal viral K plus channels as robust model systems for understanding structure/function correlations
Language: English
Abstract:

The channel proteins from Chlorella viruses are miniature versions of K+ channels; in essence they represent the pore module of complex K+ channels from eukaryotes. The combination of small size and robust function makes them good model systems for understanding basic structure/function correlates in K+ channels. The channel Kcv NTS counts only 82 amino acids per monomer and molecular dynamics simulations suggest that the channel is quasi fully embedded in the membrane bilayer. The intimate interaction between the channel protein and the surrounding bilayer offers the possibility to examine the performance of the channel in different experimental systems. We therefore performed single channel experiments in vertical and horizontal lipid bilayers as well in the membrane of native HEK-cellsystem. Furthermore we monitored channel conductance and gating in lipids with different head-groups and/or lipids with fatty acid chains of different length.

Journal or Publication Title: European biophysics journal : EBJ
Volume: 42
Number: Suppl. 1
Divisions: 10 Department of Biology
10 Department of Biology > Plant Membrane Biophysics
Date Deposited: 01 Jul 2014 08:23
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