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. 2000 Aug 1;116(2):181–190. doi: 10.1085/jgp.116.2.181

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Differential effects of neutralization of charges in extracellular dicarboxylic residues of Shaker K⁺ channels. (A) Scheme of the transmembrane topology of the α subunit of the K⁺ channel with indication of the residues mutated in this study. (B) Representative recordings of outward K⁺ currents from six different types of channels studied. In all cases, the membrane was depolarized from −80 to +20 mV during 100-ms depolarizations, and external K⁺ was 2.7 mM. Two different recordings corresponding to channel 5Q are superimposed to illustrate the variability of C-type inactivation in this mutant (*time constant, 1,970 ms; **time constant, 542 ms). Current amplitude is scaled to match the value of the current in the trace indicated with the single asterisk.