ArticleBiophysical journal2003
Role of the dielectric constants of membrane proteins and channel water in ion permeation.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- A comprehensive computational study of amino acid interactions in membrane proteins.Scientific reports · 2019Article
- A method for treating the passage of a charged hard sphere ion as it passes through a sharp dielectric boundary.The Journal of chemical physics · 2011Article
- Discretization of the induced-charge boundary integral equation.Physical review. E, Statistical, nonlinear, and soft matter physics · 2009Article
- Steric selectivity in Na channels arising from protein polarization and mobile side chains.Biophysical journal · 2007Article
- Epithelial fluid transport: protruding macromolecules and space charges can bring about electro-osmotic coupling at the tight junctions.The Journal of membrane biology · 2005Article
- On the importance of atomic fluctuations, protein flexibility, and solvent in ion permeation.The Journal of general physiology · 2004Article
- Ion permeation through the alpha-hemolysin channel: theoretical studies based on Brownian dynamics and Poisson-Nernst-Plank electrodiffusion theory.Biophysical journal · 2004Article
- Effect of dielectric interface on charge aggregation in the voltage-gated K(+) ion channel.Journal of natural science, biology, and medicineArticle
- A new approach to the selectivity of ion channels: nonlocal electrostatic consideration.Doklady. Biochemistry and biophysicsArticle
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Authors and funding
2 authors.
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Abstract
Using both analytical solutions obtained from simplified systems and numerical results from more realistic cases, we investigate the role played by the dielectric constant of membrane proteins epsilon(p) and pore water epsilon(w) in permeation of ions across channels. We show that the boundary and its curvature are the crucial factors in determining how an ion's potential energy depends on the dielectric constants near an interface. The potential energy of an ion outside a globular protein has a dominant 1/epsilon(w) dependence, but this becomes 1/epsilon(p) for an ion inside a cavity. For channels, where the boundaries are in between these two extremes, the situation is more complex. In general, we find that variations in epsilon(w) have a much larger impact on the potential energy of an ion compared to those in epsilon(p). Therefore a better understanding of the effective epsilon(w) values employed in channel models is desirable. Although the precise value of epsilon(p) is not a crucial determinant of ion permeation properties, it still needs to be chosen carefully when quantitative comparisons with data are made.
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