Alteration of the pH-dependent ion selectivity of the colicin E1 channel by site-directed mutagenesis.

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Article

Alteration of the pH-dependent ion selectivity of the colicin E1 channel by site-directed mutagenesis.

The Journal of biological chemistry - 25 Apr 1990

Jakes K S, Abrams C K, Finkelstein A, Slatin S L

Abstract excerpt

Colicin E1 is a soluble, bacteriocidal protein that forms voltage-gated channels in planar lipid bilayers. The channel-forming region of the 522-amino acid protein is near the COOH terminus, and contains a 35-amino acid hydrophobic segment which is presumed to be important in interacting with the...

Topics

Amino Acid Sequence
Base Sequence
Colicins
Escherichia coli
Escherichia coli Proteins
Genes, Bacterial
Hydrogen-Ion Concentration
Iodoacetamide
Iodoacetates
Iodoacetic Acid
Ion Channels
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Lipid Bilayers

Membrane Potentials

Molecular Sequence Data

Mutation

Oligonucleotide Probes

Plasmids

Source

Open in PubMed

Identifiers

PMID: 1691183

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1691183-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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