ArticleBiophysical journal2010
Ionic partition and transport in multi-ionic channels: a molecular dynamics simulation study of the OmpF bacterial porin.
Article in Biophysical journal, 2010. 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.
- Electrophysiological Properties from Computations at a Single Voltage: Testing Theory with Stochastic Simulations.Entropy (Basel, Switzerland) · 2021Article
- Understanding the ionic activity and conductivity value differences between random copolymer electrolytes and block copolymer electrolytes of the same chemistry.RSC advances · 2021Article
- Ionophore constructed from non-covalent assembly of a G-quadruplex and liponucleoside transports KNature communications · 2020Article
- Validity of the Electrodiffusion Model for Calculating Conductance of Simple Ion Channels.The journal of physical chemistry. B · 2017Article
- Role of Electroosmosis in the Permeation of Neutral Molecules: CymA and Cyclodextrin as an Example.Biophysical journal · 2016Article
- Understanding Voltage Gating of Providencia stuartii Porins at Atomic Level.PLoS computational biology · 2015Article
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Divalent Metal Ion Transport across Large Biological Ion Channels and Their Effect on Conductance and Selectivity.Biochemistry research international · 2012Article
- Molecular dynamics simulation of the antiamoebin ion channel: linking structure and conductance.Biophysical journal · 2011Article
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Authors and funding
3 authors.
Funding
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Abstract
We performed all-atom molecular dynamics simulations studying the partition of ions and the ionic current through the bacterial porin OmpF and two selected mutants. The study is motivated by new, interesting experimental findings concerning their selectivity and conductance behavior at neutral pH. The mutations considered here are designed to study the effect of removal of negative charges present in the constriction zone of the wild-type OmpF channel (which contains, on one side, a cluster with three positive residues, and on the other side, two negatively charged residues). Our results show that these mutations induce an exclusion of cations from the constriction zone of the channel, substantially reducing the flow of cations. In fact, the partition of ions inside the mutant channels is strongly inhomogeneous, with regions containing an excess of cations and regions containing an excess of anions. Interestingly, the overall number of cations inside the channel is larger than the number of anions, this excess being different for each protein channel. We found that the differences in ionic charge inside these channels are justified by the differences in electric charge between the wild-type OmpF and the mutants, following an electroneutral balance.
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