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Cited by 345

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Kcsa

Open access
LeMasurier, Meredith, Heginbotham, Lise, Miller, Christopher·2001·The Journal of General Physiology

Abstract

Ion conduction and selectivity properties of KcsA, a bacterial ion channel of known structure, were studied in a planar lipid bilayer system at the single-channel level. Selectivity sequences for permeant ions were determined by symmetrical solution conductance (K+ > Rb+, NH4+, Tl+ ≫ Cs+, Na+, Li+) and by reversal potentials under bi-ionic or mixed-ion conditions (Tl+ > K+ > Rb+ > NH4+ ≫ Na+, Li+). Determination of reversal potentials with submillivolt accuracy shows that K+ is over 150-fold more permeant than Na+. Variation of conductance with concentration under symmetrical salt conditions is complex, with at least two ion-binding processes revealing themselves: a high affinity process below 20 mM and a low affinity process over the range 100–1,000 mM. These properties are analogous to those seen in many eukaryotic K+ channels, and they establish KcsA as a faithful structural model for ion permeation in eukaryotic K+ channels.

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Metadata

Authors
LeMasurier, M., Heginbotham, L., & Miller, C.
Venue
The Journal of General Physiology
Published
2001-08-27
Volume
118
Issue
3
Pages
303-314
ISSN
  • 0022-1295 (ISSN-L)
  • 1540-7748
OpenAlex
W2109258309
Cited by
345
References
0
FWCI
5.54
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Kcsa. https://app.cochat.ai/papers/10.1085/jgp.118.3.303
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LeMasurier, M., Heginbotham, L., & Miller, C. (2001). Kcsa. The Journal of General Physiology. https://doi.org/10.1085/jgp.118.3.303

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.