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Two-dimensional solid-state NMR applied to a chimeric potassium channel.

Adam Lange·Karin Giller·Olaf Pongs·Stefan Becker·Marc Baldus
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Abstract

Solid-state NMR (ssNMR) represents a spectroscopic method to study membrane protein structure and dynamics in lipid bilayers. We present two-dimensional correlation experiments conducted on a fully [13C,15N] labeled version of a chimeric potassium (KcsA-Kv1.3) channel. Data obtained by using two different ion concentrations suggest a structural conservation of the selectivity filter region. SsNMR experiments conducted at two different temperatures point to differential molecular dynamics of the channel.

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Bacterial ProteinsCarbon IsotopesCloning, MolecularKv1.3 Potassium ChannelMembrane ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPotassium ChannelsRecombinant Fusion ProteinsTemperatureJournal ArticleResearch Support, Non-U.S. Gov't

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Adam Lange, Karin Giller, Olaf Pongs, Stefan Becker, Marc Baldus. 2006. Two-dimensional solid-state NMR applied to a chimeric potassium channel.. https://doi.org/10.1080/10799890600932188

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