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Updated: Jun 6, 2026

High Resolution Physical Characterization of Single Metallic Nanoparticles
Published on: June 28, 2019
Linearity, saturation and blocking in a large multiionic channel: divalent cation modulation of the OmpF porin
Elena García-Giménez1, M Lidón López, Vicente M Aguilella
1Laboratory of Molecular Biophysics, Department of Physics, Universitat Jaume I, Av. Sos Baynat s/n, 12080 Castellón, Spain.
Abstract:
Measurement of unitary conductance is a fundamental step in the characterization of a protein ion channel permeabilizing a membrane. We study here the effect of salts of divalent cations on the OmpF channel conductance with a particular emphasis in dissecting the role of the electrolyte itself, the role of the counterion accumulation induced by the protein channel charges and other effects not found in salts of monovalent cations. We show that current saturation and blocking are not exclusive properties of narrow (single-file) ion channels but may be observed in large, multiionic channels like bacterial porins. Single-channel conductance measurements performed over a wide range of salt concentrations (up to 3 M) combined with continuum electrodiffusion calculations demonstrate that current saturation cannot be simply ascribed to ion interaction with protein channel residues.
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