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Updated: Jun 4, 2026

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
Published on: July 3, 2018
Changes in ion channel geometry resolved to sub-ångström precision via single molecule mass spectrometry
Joseph W F Robertson1, John J Kasianowicz, Joseph E Reiner
1Semiconductor Electronics Division, Electronics and Electrical Engineering Laboratory, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA.
Abstract:
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%.
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