Two-dimensional solid-state NMR applied to a chimeric potassium channel.
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.
Lange
Adam
A
Department for NMR-Based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
Giller
Karin
K
Pongs
Olaf
O
Becker
Stefan
S
Baldus
Marc
M
D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D003001:Cloning, Molecular; D051664:Kv1.3 Potassium Channel / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D015221:Potassium Channels / Q000737:chemistry*; D011993:Recombinant Fusion Proteins; D013696:Temperature
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D051664:Kv1.3 Potassium Channel; D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D015221:Potassium Channels; D011993:Recombinant Fusion Proteins; C107790:prokaryotic potassium channel