Linearity, saturation and blocking in a large multiionic channel: divalent cation modulation of the OmpF porin conductance
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Scholar |
Otros documentos de la autoría: García Giménez, Elena; López Peris, María Lidón; Aguilella, Vicente; Alcaraz, Antonio
Metadatos
Mostrar el registro completo del ítemcomunitat-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 |
Metadatos
Título
Linearity, saturation and blocking in a large multiionic channel: divalent cation modulation of the OmpF porin conductanceFecha de publicación
2011-01Editor
ElsevierISSN
0006-291X; 1090-2104Cita bibliográfica
Biochemical and Biophysical Research Communications (7 Jan. 2011), vol. 404, no. 1, 330–334Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://www.sciencedirect.com/science/article/pii/S0006291X10021935Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
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. [-]
Derechos de acceso
© 2010 Elsevier Inc. All rights reserved
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