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Issue 3, 2011
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Insights on the permeability of wide protein channels: measurement and interpretation of ion selectivity

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Abstract

Ion channels are hollow proteins that have evolved to exhibit discrimination between charged solutes. This property, known as ion selectivity is critical for several biological functions. By using the bacterial porin OmpF as a model system of wide protein channels, we demonstrate that significant insights can be gained when selectivity measurements are combined with electrodiffusion continuum models and simulations based on the atomic structure. A correct interpretation of the mechanisms ruling the many sources of channel discrimination is a first, indispensable step for the understanding of the controlled movement of ions into or out of cells characteristic of many physiological processes. We conclude that the scattered information gathered from several independent approaches should be appropriately merged to provide a unified and coherent picture of the channel selectivity.

Graphical abstract: Insights on the permeability of wide protein channels: measurement and interpretation of ion selectivity

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Publication details

The article was received on 31 May 2010, accepted on 12 Oct 2010 and first published on 06 Dec 2010


Article type: Review Article
DOI: 10.1039/C0IB00048E
Citation: Integr. Biol., 2011,3, 159-172
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    Insights on the permeability of wide protein channels: measurement and interpretation of ion selectivity

    V. M. Aguilella, M. Queralt-Martín, M. Aguilella-Arzo and A. Alcaraz, Integr. Biol., 2011, 3, 159
    DOI: 10.1039/C0IB00048E

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