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Article

Adventures in membrane protein topology. A study of the membrane-bound state of colicin E1.

The Journal of biological chemistry - 27 Aug 1999

Tory M C, Merrill A R

Abstract excerpt

The molecular aggregate size of the closed state of the colicin E1 channel was determined by fluorescence resonance energy transfer experiments involving a fluorescence donor (three tryptophans, wild-type protein) and a fluorescence acceptor (5-(((acetyl)amino)ethyl)aminonaphthalene-1-sulfonic acid (AEDANS), Trp-deficient protein). There was no evidence of energy transfer between the donor and acceptor species...

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Source

Identifiers

PMID: 10455117
DOI: 10.1074/jbc.274.35.24539

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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Adventures in membrane protein topology. A study of the membrane-bound state of colicin E1.PMID 10455117Read ↗

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Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering.Semantic proximity Read ↗

Protein translocation across planar bilayers by the colicin Ia channel-forming domain: where will it end?Semantic proximity Read ↗

Determining the membrane topology of proteins: insertion pathway of a transmembrane helix of annexin 12.Semantic proximity Read ↗

Fine-tuning the topology of a polytopic membrane protein: role of positively and negatively charged amino acids.Semantic proximity Read ↗

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