Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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




Journal article


Biophys J

Publication Date





770 - 778


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