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Article

Electrostatic interactions between transmembrane segments mediate folding of Shaker K+ channel subunits.

Biophysical journal - 1 Apr 1997

Tiwari-Woodruff S K, Schulteis C T, Mock A F, Papazian D M

Abstract excerpt

In voltage-dependent Shaker K+ channels, charged residues E293 in transmembrane segment S2 and R365, R368, and R371 in S4 contribute significantly to the gating charge movement that accompanies activation. Using an intragenic suppression strategy, we have now probed for structural interaction between transmembrane segments S2, S3, and S4 in Shaker channels. Charge reversal mutations of E283 in S2 and K374 in S4...

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Identifiers

PMID: 9083655
DOI: 10.1016/S0006-3495(97)78797-6
PMCID: PMC1184345

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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