Do Amino Acid Substitutions Alter the Structure of Gramicidin Channels? Chemistry at the Single Molecule Level
- 1 January 1988
- book chapter
- Published by Springer Nature
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Temperature-jump and voltage-jump experiments at planar lipid membranes support an aggregational (micellar) model of the gramicidin A ion channelThe Journal of Membrane Biology, 1986
- 1H‐NMR study of gramicidin A transmembrane ion channelFEBS Letters, 1985
- The gramicidin A channelFEBS Letters, 1984
- Computer building of β‐helical polypeptide modelsBiopolymers, 1984
- Theoretical conformational analysis of the Gramicidin a transmembrane channel. I. Helix sense and energetics of head‐to‐head dimerizationJournal of Computational Chemistry, 1983
- Is the Gramicidin A Transmembrane Channel Single-Stranded or Double-Stranded Helix? A Simple Unequivocal DeterminationScience, 1983
- Structural homology of Torpedo californica acetylcholine receptor subunitsNature, 1983
- Conduction and selectivity in potassium channelsThe Journal of Membrane Biology, 1983
- The dimeric nature of the gramicidin A transmembrane channel: Conductance and fluorescence energy transfer studies of hybrid channelsJournal of Molecular Biology, 1977
- Channel formation kinetics of gramicidin A in lipid bilayer membranesThe Journal of Membrane Biology, 1973