Changes in ion channel geometry resolved to sub-ångström precision via single molecule mass spectrometry.

The ion channel formed by Staphylococcus aureus alpha-hemolysin switches between multiple open conducting states. We describe a method for precisely estimating the changes in the ion channel geometry that correspond to these different states. Experimentally, we observed 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 is proposed for determining changes in channel length of 4.2% and in cross-sectional area of -0.4%.