Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Methionine mutations of outer membrane protein X influence structural stability and beta-barrel unfolding.

PloS one - 1 Jan 2013

Chaturvedi Deepti, Mahalakshmi Radhakrishnan

Abstract excerpt

We report the biochemical and biophysical characterization of outer membrane protein X (OmpX), an eight-stranded transmembrane β-barrel from E. coli, and compare the barrel behavior with a mutant devoid of methionine residues. Transmembrane outer membrane proteins of bacterial origin are known to display high tolerance to sequence rearrangements and mutations. Our studies with the triple mutant of OmpX that is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Outer Membrane Proteins
Share to Hydrolases
Share to Methionine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Protein Stability

Share to Protein Structure, Secondary

Share to Protein Unfolding

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 24265768
DOI: 10.1371/journal.pone.0079351
PMCID: PMC3827151

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Methionine mutations of outer membrane protein X influence structural stability and beta-barrel unfolding.PMID 24265768Read ↗

Dimer-to-tetramer transformation: loop excision dramatically alters structure and stability of the ROP four alpha-helix bundle protein.Semantic proximity Read ↗

Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA.Semantic proximity Read ↗

Replacement of tyr62 by trp in the designer protein milk bundle-1 results in significant improvement of conformational stability.Semantic proximity Read ↗

The hydrophobic core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions.Semantic proximity Read ↗

In vivo impact of Met221 substitution in GOB metallo-β-lactamase.Semantic proximity Read ↗

Expression and spectroscopic analysis of a mutant hepatitis B virus onco-protein HBx without cysteine residues.Semantic proximity Read ↗

Position-Specific contribution of interface tryptophans on membrane protein energetics.Semantic proximity Read ↗

Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA.Semantic proximity Read ↗

His(20) provides the sole functionally significant side chain in the essential TonB transmembrane domain.Semantic proximity Read ↗

Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state.Semantic proximity Read ↗

Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress.Semantic proximity Read ↗

Partial suppression of an Escherichia coli TonB transmembrane domain mutation (delta V17) by a missense mutation in ExbB.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.