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Article

The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects.

Biophysical journal - 8 Jan 2013

Schwaiger Christine S, Liin Sara I, Elinder Fredrik, Lindahl Erik

Abstract excerpt

Voltage-gated ion channels are crucial for regulation of electric activity of excitable tissues such as nerve cells, and play important roles in many diseases. During activation, the charged S4 segment in the voltage sensor domain translates across a hydrophobic core forming a barrier for the gating charges. This barrier is critical for channel function, and a conserved phenylalanine in segment S2 has previously...

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Share to Conserved Sequence
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 23332060
DOI: 10.1016/j.bpj.2012.11.3827
PMCID: PMC3540256

Provenance

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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