Article
Electrostatic interactions between transmembrane segments mediate folding of Shaker K+ channel subunits.
Biophysical journal - 1 Apr 1997
Tiwari-Woodruff S K, Schulteis C T, Mock A F, Papazian D M
Abstract excerpt
In voltage-dependent Shaker K+ channels, charged residues E293 in transmembrane segment S2 and R365, R368, and R371 in S4 contribute significantly to the gating charge movement that accompanies activation. Using an intragenic suppression strategy, we have now probed for structural interaction bet...
Topics
- Animals
- Cell Membrane
- Electrophoresis, Polyacrylamide Gel
- Electrophysiology
- Gene Expression
- Ion Channel Gating
- Kinetics
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Oocytes
- Patch-Clamp Techniques
- Polymerase Chain Reaction
- Potassium Channels
- Protein Folding
- Protein Structure, Secondary
- Shaker Superfamily of Potassium Channels
- Xenopus
