Interactions of phospholipids with the potassium channel KcsA.

@article{Williamson2002InteractionsOP,
  title={Interactions of phospholipids with the potassium channel KcsA.},
  author={I. H. M. Williamson and Simon J Alvis and J. Malcolm East and Anthony G. Lee},
  journal={Biophysical journal},
  year={2002},
  volume={83 4},
  pages={2026-38}
}
The potassium channel KcsA from Streptomyces lividans has been reconstituted into bilayers of phosphatidylcholines and fluorescence spectroscopy has been used to characterize the response of KcsA to changes in bilayer thickness. The Trp residues in KcsA form two bands, one on each side of the membrane. Trp fluorescence emission spectra and the proportion of the Trp fluorescence intensity quenchable by I(-) hardly vary in the lipid chain length range C10 to C24, suggesting efficient hydrophobic… CONTINUE READING