Covalent dimers of alamethicin form conducting structures with gating properties that permit measurement of current-voltage (I-V) relationships during the lifetime of a single channel. These I-V curves demonstrate that the alamethicin channel is a rectifier that passes current preferentially, with voltages of the same sign as that of the voltage that induced opening of the channel. The degree of rectification depends on the salt concentration; single-channel I-V relationships become almost linear in 3 M potassium chloride. These properties may be qualitatively understood by using Poisson-Nernst-Planck theory and a modeled structure of the alamethicin pore
Alamethicin is an α-helical peptide that forms voltage-activated ion channels. Experimental data sug...
We have examined the causes of the asymmetry of the current-voltage curve induced by addition of ala...
Alamethicin and its analogs from cation selective, multi-conductance channels in lipid bilayers. The...
Covalent dimers of alamethicin form conducting structures with gating properties that permit measure...
ABSTRACT Covalent dimers of alamethicin form conducting structures with gating properties that permi...
Molecular structures of transmembrane channels formed by alamethicin polypeptide aggregates were ana...
Alamethicin, a 20-amino acid peptide, has been studied for a number of years as a model for voltage-...
AbstractA covalent dimer of alamethicin Rf30 was synthesized by linking the N-termini by a disulfide...
Alamethicin at a concentration of 2 micrograms/ml on one side of a lipid bilayer, formed at the tip ...
AbstractSeveral analogues of the channel-forming peptaibol alamethicin have been demonstrated to exh...
The ion currents induced by alamethicin were investigated in unilamellar vesicles using electron par...
Alamethicin, a 20-residue peptaibol, induces voltage-dependent ion channels in lipid bilayers accord...
AbstractIn order to test the influence of chemical modifications designed to allow covalent coupling...
AbstractAlamethicin, a member of the peptaibol family of antibiotics, is a typical channel-forming p...
Channel access resistance has been measured to estimate the characteristic size of a single ion chan...
Alamethicin is an α-helical peptide that forms voltage-activated ion channels. Experimental data sug...
We have examined the causes of the asymmetry of the current-voltage curve induced by addition of ala...
Alamethicin and its analogs from cation selective, multi-conductance channels in lipid bilayers. The...
Covalent dimers of alamethicin form conducting structures with gating properties that permit measure...
ABSTRACT Covalent dimers of alamethicin form conducting structures with gating properties that permi...
Molecular structures of transmembrane channels formed by alamethicin polypeptide aggregates were ana...
Alamethicin, a 20-amino acid peptide, has been studied for a number of years as a model for voltage-...
AbstractA covalent dimer of alamethicin Rf30 was synthesized by linking the N-termini by a disulfide...
Alamethicin at a concentration of 2 micrograms/ml on one side of a lipid bilayer, formed at the tip ...
AbstractSeveral analogues of the channel-forming peptaibol alamethicin have been demonstrated to exh...
The ion currents induced by alamethicin were investigated in unilamellar vesicles using electron par...
Alamethicin, a 20-residue peptaibol, induces voltage-dependent ion channels in lipid bilayers accord...
AbstractIn order to test the influence of chemical modifications designed to allow covalent coupling...
AbstractAlamethicin, a member of the peptaibol family of antibiotics, is a typical channel-forming p...
Channel access resistance has been measured to estimate the characteristic size of a single ion chan...
Alamethicin is an α-helical peptide that forms voltage-activated ion channels. Experimental data sug...
We have examined the causes of the asymmetry of the current-voltage curve induced by addition of ala...
Alamethicin and its analogs from cation selective, multi-conductance channels in lipid bilayers. The...