Insights on the permeability of wide protein channels: measurement and interpretation of ion selectivity
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Show full item recordcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/2507
comunitat-uji-handle3:10234/6973
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http://dx.doi.org/10.1039/C0IB00048E |
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Title
Insights on the permeability of wide protein channels: measurement and interpretation of ion selectivityDate
2012-10-11Publisher
Royal Society of ChemistryISSN
1757-9694Bibliographic citation
Integrative Biology, 2011, March, vol. 3, no. 3Type
info:eu-repo/semantics/articlePublisher version
http://pubs.rsc.org/en/content/articlelanding/2011/ib/c0ib00048eVersion
info:eu-repo/semantics/publishedVersionSubject
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 ... [+]
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. [-]
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© Royal Society of Chemistry 2012
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