ArticleBiophysical journal2011
Comparative study of the energetics of ion permeation in Kv1.2 and KcsA potassium channels.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Ion Channel Reaction Networks: Dielectric Screening and the Importance of Off-Pathway Flux.Journal of chemical theory and computation · 2025Article
- Molecular simulation of the Kv7.4[ΔS269] mutant channel reveals that ion conduction in the cavity is perturbed due to hydrophobic gating.Biochemistry and biophysics reports · 2021Article
- Queueing arrival and release mechanism for KThe journal of physiological sciences : JPS · 2019Article
- Computational Study of the Loss-of-Function Mutations in the Kv1.5 Channel Associated with Atrial Fibrillation.ACS omega · 2018Article
- Quantitative Assessment of the Energetics of Dopamine Translocation by Human Dopamine Transporter.The journal of physical chemistry. B · 2018Article
- Article
- Energetics of Multi-Ion Conduction Pathways in Potassium Ion Channels.Journal of chemical theory and computation · 2013Article
- Detailed Examination of a Single Conduction Event in a Potassium Channel.The journal of physical chemistry letters · 2013Article
- Computational studies of marine toxins targeting ion channels.Marine drugs · 2013Review
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- High-risk long QT syndrome mutations in the Kv7.1 (KCNQ1) pore disrupt the molecular basis for rapid K(+) permeation.Biochemistry · 2012Article
- Molecular dynamics simulations of membrane proteins.Biophysical reviews · 2012Review
- Modeling the binding of three toxins to the voltage-gated potassium channel (Kv1.3).Biophysical journal · 2011Article
- Blockade of permeation by potassium but normal gating of the G628S nonconducting hERG channel mutant.Biophysical journal · 2011Article
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Authors and funding
2 authors.
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Abstract
Biological ion channels rely on a multi-ion transport mechanism for fast yet selective permeation of ions. The crystal structure of the KcsA potassium channel provided the first microscopic picture of this process. A similar mechanism is assumed to operate in all potassium channels, but the validity of this assumption has not been well investigated. Here, we examine the energetics of ion permeation in Shaker Kv1.2 and KcsA channels, which exemplify the six-transmembrane voltage-gated and two-transmembrane inward-rectifier channels. We study the feasibility of binding a third ion to the filter and the concerted motion of ions in the channel by constructing the potential of mean force for K(+) ions in various configurations. For both channels, we find that a pair of K(+) ions can move almost freely within the filter, but a relatively large free-energy barrier hinders the K(+) ion from stepping outside the filter. We discuss the effect of the CMAP dihedral energy correction that was recently incorporated into the CHARMM force field on ion permeation dynamics.
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