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Abstract
The ion channel formed by Staphylococcus aureus alpha-hemolysin switches betweenmultiple open conducting states. We describe a method for precisely estimating the changesin the ion channel geometry that correspond to these different states. Experimentally, weobserved that the permeability of a single channel to differently sized poly(ethylene glycol)molecules depends on the magnitude of the open state conductance. A simple theory isproposed for determining changes in channel length of 4.2% and in cross-sectional area of − 0.4%.
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