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

J Recept Signal Transduct Res. 2006;26(5-6):379-93. doi: 10.1080/10799890600932188.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Carbon Isotopes
  • Cloning, Molecular
  • Kv1.3 Potassium Channel / chemistry*
  • Membrane Proteins / chemistry
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Potassium Channels / chemistry*
  • Recombinant Fusion Proteins
  • Temperature

Substances

  • Bacterial Proteins
  • Carbon Isotopes
  • Kv1.3 Potassium Channel
  • Membrane Proteins
  • Nitrogen Isotopes
  • Potassium Channels
  • Recombinant Fusion Proteins
  • prokaryotic potassium channel