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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.

Original publication

DOI

10.1016/S0006-3495(97)78109-8

Type

Journal article

Journal

Biophys J

Publication Date

08/1997

Volume

73

Pages

770 - 778

Keywords

Alamethicin, Amino Acid Sequence, Dimerization, Ion Channel Gating, Kinetics, Lipid Bilayers, Membrane Potentials, Models, Biological, Models, Structural, Molecular Sequence Data, Phosphatidylcholines, Potassium Channels, Potassium Chloride, Protein Structure, Secondary, Static Electricity, Thermodynamics