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Article

Disulfide bond tethering of extracellular loops does not affect the closure of OmpF porin at acidic pH.

Proteins - 1 Nov 2010

Wager Beau, Baslé Arnaud, Delcour Anne H

Abstract excerpt

The permeability of the outer membrane of gram-negative bacteria is essentially controlled by pore-forming proteins of the porin family. The trimeric E. coli porin OmpF is assembled as a triple β-barrel, where each monomer contains a central pore and extracellular loops. Electrophysiological analysis of the behavior of OmpF at acidic pH reveals that the protein undergoes a conformational change leading to the...

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PMID: 20665474
DOI: 10.1002/prot.22807

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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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