ArticleBiochimica et biophysica acta2016
Multi-ion free energy landscapes underscore the microscopic mechanism of ion selectivity in the KcsA channel.
Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 46 citations in OpenAlex.
- Force field sensitivity of ion occupancy in potassium channels.Biophysical journal · 2026Article
- Terahertz Modulation of Biomolecular Dynamics: Physical Mechanisms, Biological Implications, and Future Challenges.Research (Washington, D.C.) · 2026Review
- Deciphering CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Ion and water permeation through claudin-10b and claudin-15 paracellular channels.Computational and structural biotechnology journal · 2024Article
- The Molecular Mechanism of Ion Selectivity in Nanopores.Molecules (Basel, Switzerland) · 2024Article
- Effect of THz Waves of Different Orientations on KInternational journal of molecular sciences · 2023Article
- Regulation of Ion Permeation of the KcsA Channel by Applied Midinfrared Field.International journal of molecular sciences · 2022Article
- Hydrated Anions: From Clusters to Bulk Solution with Quasi-Chemical Theory.Accounts of chemical research · 2022Article
- Ion permeation, selectivity, and electronic polarization in fluoride channels.Biophysical journal · 2022Article
- Computational methods and theory for ion channel research.Advances in physics: X · 2022Article
- Energy landscape of the SARS-CoV-2 reveals extensive conformational heterogeneity.Current research in structural biology · 2022Article
- Weak Cation Selectivity in HCN Channels Results From KFunction (Oxford, England) · 2022Article
- Thermodynamics of ion binding and occupancy in potassium channels.Chemical science · 2021Article
- Molecular Simulations of Hydrophobic Gating of Pentameric Ligand Gated Ion Channels: Insights into Water and Ions.The journal of physical chemistry. B · 2021Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Retrieving functional pathways of biomolecules from single-particle snapshots.Nature communications · 2020Article
- Selectivity filter modalities and rapid inactivation of the hERG1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Rapid constriction of the selectivity filter underlies C-type inactivation in the KcsA potassium channel.The Journal of general physiology · 2018Article
- Direct knock-on of desolvated ions governs strict ion selectivity in KNature chemistry · 2018Article
- The permeation mechanism of organic cations through a CNG mimic channel.PLoS computational biology · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Potassium (K(+)) channels are transmembrane proteins that passively and selectively allow K(+) ions to flow through them, after opening in response to an external stimulus. One of the most critical functional aspects of their function is their ability to remain very selective for K(+) over Na(+) while allowing high-throughput ion conduction at a rate close to the diffusion limit. Classically, it is assumed that the free energy difference between K(+) and Na(+) in the pore relative to the bulk solution is the critical quantity at the origin of selectivity. This is the thermodynamic view of ion selectivity. An alternative view assumes that kinetic factors play the dominant role. Recent results from a number of studies have also highlighted the great importance of the multi-ion single file on the selectivity of K(+) channels. The data indicate that having multiple K(+) ions bound simultaneously is required for selective K(+) conduction, and that a reduction in the number of bound K(+) ions destroys the multi-ion selectivity mechanism utilized by K(+) channels. In the present study, multi-ion potential of mean force molecular dynamics computations are carried out to clarify the mechanism of ion selectivity in the KcsA channel. The computations show that the multi-ion character of the permeation process is a critical element for establishing the selective ion conductivity through K(+)-channels. This article is part of a Special Issue entitled: Membrane Proteins edited by J.C. Gumbart and Sergei Noskov.
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