Linearity, saturation and blocking in a large multiionic channel: divalent cation modulation of the OmpF porin conductance
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Other documents of the author: García Giménez, Elena; López Peris, María Lidón; Aguilella, Vicente; Alcaraz, Antonio
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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/10.1016/j.bbrc.2010.11.118 |
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Title
Linearity, saturation and blocking in a large multiionic channel: divalent cation modulation of the OmpF porin conductanceDate
2011-01Publisher
ElsevierISSN
0006-291X; 1090-2104Bibliographic citation
Biochemical and Biophysical Research Communications (7 Jan. 2011), vol. 404, no. 1, 330–334Type
info:eu-repo/semantics/articlePublisher version
http://www.sciencedirect.com/science/article/pii/S0006291X10021935Version
info:eu-repo/semantics/publishedVersionSubject
Abstract
Measurement of unitary conductance is a fundamental step in the characterization of a protein ion channelpermeabilizing a membrane. We study here the effect of salts of divalent cations on the OmpF channelconductance ... [+]
Measurement of unitary conductance is a fundamental step in the characterization of a protein ion channelpermeabilizing a membrane. We study here the effect of salts of divalent cations on the OmpF channelconductance 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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© 2010 Elsevier Inc. All rights reserved
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