How to open a proton pore-more than S4?
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Updated: Jul 12, 2026

Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
Marcel P Goldschen-Ohm1, Baron Chanda1
1Departments of Neuroscience and Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin, USA.
Abstract:
Pioneering studies in voltage-gated potassium channels have described movement of the voltage-sensing domain (VSD) S4 helix across the membrane electric field in molecular detail, but much less is known regarding opening of the intrinsic proton pore within VSDs of voltage-dependent proton channels. By systematically probing local kinematics, a new study reveals that movements in helix S1 correlate with pore opening and are distinct from voltage-sensing movements of the charged S4 segment.
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