Access resistance in protein nanopores. A structure-based computational approach
Metadatos
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comunitat-uji-handle2:10234/2507
comunitat-uji-handle3:10234/6973
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INVESTIGACIONMetadatos
Título
Access resistance in protein nanopores. A structure-based computational approachFecha de publicación
2020-02Editor
ElsevierISSN
1567-5394Cita bibliográfica
AGUILELLA-ARZO, Marcel; AGUILELLA, Vicente M. Access resistance in protein nanopores. A structure-based computational approach. Bioelectrochemistry, 2020, vol. 131, p. 107371Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
https://www.sciencedirect.com/science/article/pii/S1567539419305420Versión
info:eu-repo/semantics/submittedVersionPalabras clave / Materias
Resumen
Single-channel conductance measurements in biological pores have demonstrated the importance of interfacial effects in nanopores, particularly in protein channels with low aspect ratio (length over aperture radius). ... [+]
Single-channel conductance measurements in biological pores have demonstrated the importance of interfacial effects in nanopores, particularly in protein channels with low aspect ratio (length over aperture radius). Access resistance (AR), the contribution to the total measured resistance arising from the electrodiffusive limitation that ions experience in passing from bulk solution to confinement within the pore, becomes essential in the description of ionic transport across these biological channels. Common analytical estimates of AR are based on idealized nanopore models, cylindrical in shape, electrically neutral and embedded in a neutral substrate. Here we calculate the AR of five protein channels by using their atomic structure and a mean-field approach based on solving 3D Poisson and Nernst-Planck equations. Our approach accounts for the influence of the protein charged ionizable residues, the geometry of the pore mouth and the ion concentration gradients near the pore. We compare numerical calculations with the few available AR measurements and show for several protein channels that analytical predictions tend to overestimate AR for physiological concentrations and below. We also discuss the relationship between AR and the size of the channel aperture in single-pore channels and three-pore channels and demonstrate that in the latter case, there is an enhancement of AR. [-]
Publicado en
Bioelectrochemistry, 2020, vol. 131Proyecto de investigación
Government of Spain: project no. FIS2016-75257-P AEI/FEDER, UE; Universitat Jaume I: project no. UJI-B2018-53Derechos de acceso
Copyright © Elsevier B.V.
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