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Article

IR-spectroscopic characterization of an elongated OmpG mutant.

Archives of biochemistry and biophysics - 15 Jun 2015

Korkmaz Filiz, van Pee Katharina, Yildiz Özkan

Abstract excerpt

OmpG is a nonselective, pH dependent outer membrane protein from Escherichia coli. It consists of 281 residues, forming a 14-stranded β-sheet structure. In this study, OmpG is extended by 38 amino acids to produce a 16-stranded β-barrel (OmpG-16S). The resulting protein is investigated by IR-spectroscopy. The secondary structure, pH-dependent opening/closing mechanism, buffer accessibility and thermal stability...

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Share to Bacterial Outer Membrane Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 25958106
DOI: 10.1016/j.abb.2015.04.010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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