Abstract
The current-voltage relationship of a single Staphylococcus aureus alpha-hemolysin (alphaHL) channel is nonlinear, rectifying, and depends on the bulk pH and the ionic strength. The data are described qualitatively by a simple one-dimensional Nernst-Planck analysis in which the fixed charges inside and near the pore's entrances affect the transport of ions through the channel. The distances of these fixed charges from one of the channel's entrances are obtained from the channel's crystal structure. The model demonstrates that rectification of monovalent ion flow through the alphaHL channel can be related to the asymmetry in the location of the ionizable amino acid side chains.
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