Ion channel conductance measurements on a silicon-based platform

S. J. Wilk; S. Aboud; L. Petrossian; Michael Goryll; J. M. Tang; R. S. Eisenberg; Marco Saraniti; Stephen Goodnick; Trevor Thornton

doi:10.1088/1742-6596/38/1/006

Ion channel conductance measurements on a silicon-based platform

S. J. Wilk, S. Aboud, L. Petrossian, Michael Goryll, J. M. Tang, R. S. Eisenberg, Marco Saraniti, Stephen Goodnick, Trevor Thornton

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4 Scopus citations

Abstract

Conductance measurements of the transmembrane porin protein OmpF as a function of pH and bath concentration have been made with both a microfabricated silicon substrate device and a commercially available polystyrene aperture. Ion transport through the channel was simulated in atomic detail: the measured current was compared with theoretically calculated current, using a Brownian Dynamics kernel coupled to the Poisson equation by a P3M force field. The explicit protein structure and fixed charge distribution in the protein are calculated using the molecular dynamics code, GROMACS. Reasonable agreement is obtained in the simulated versus measured conductance over the range of experimental concentrations studied.

Original language	English (US)
Pages (from-to)	21-24
Number of pages	4
Journal	Journal of Physics: Conference Series
Volume	38
Issue number	1
DOIs	https://doi.org/10.1088/1742-6596/38/1/006
State	Published - May 10 2006

ASJC Scopus subject areas

Physics and Astronomy(all)

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title = "Ion channel conductance measurements on a silicon-based platform",

abstract = "Conductance measurements of the transmembrane porin protein OmpF as a function of pH and bath concentration have been made with both a microfabricated silicon substrate device and a commercially available polystyrene aperture. Ion transport through the channel was simulated in atomic detail: the measured current was compared with theoretically calculated current, using a Brownian Dynamics kernel coupled to the Poisson equation by a P3M force field. The explicit protein structure and fixed charge distribution in the protein are calculated using the molecular dynamics code, GROMACS. Reasonable agreement is obtained in the simulated versus measured conductance over the range of experimental concentrations studied.",

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AU - Wilk, S. J.

AU - Aboud, S.

AU - Petrossian, L.

AU - Goryll, Michael

AU - Tang, J. M.

AU - Eisenberg, R. S.

AU - Saraniti, Marco

AU - Goodnick, Stephen

AU - Thornton, Trevor

PY - 2006/5/10

Y1 - 2006/5/10

N2 - Conductance measurements of the transmembrane porin protein OmpF as a function of pH and bath concentration have been made with both a microfabricated silicon substrate device and a commercially available polystyrene aperture. Ion transport through the channel was simulated in atomic detail: the measured current was compared with theoretically calculated current, using a Brownian Dynamics kernel coupled to the Poisson equation by a P3M force field. The explicit protein structure and fixed charge distribution in the protein are calculated using the molecular dynamics code, GROMACS. Reasonable agreement is obtained in the simulated versus measured conductance over the range of experimental concentrations studied.

AB - Conductance measurements of the transmembrane porin protein OmpF as a function of pH and bath concentration have been made with both a microfabricated silicon substrate device and a commercially available polystyrene aperture. Ion transport through the channel was simulated in atomic detail: the measured current was compared with theoretically calculated current, using a Brownian Dynamics kernel coupled to the Poisson equation by a P3M force field. The explicit protein structure and fixed charge distribution in the protein are calculated using the molecular dynamics code, GROMACS. Reasonable agreement is obtained in the simulated versus measured conductance over the range of experimental concentrations studied.

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Ion channel conductance measurements on a silicon-based platform

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