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

Association of neighboring β-strands of outer membrane protein A in lipid bilayers revealed by site-directed fluorescence quenching.

Journal of molecular biology - 25 Mar 2011

Kleinschmidt Jörg H, Bulieris Paula V, Qu Jian, Dogterom Marileen, den Blaauwen Tanneke

Abstract excerpt

We present a detailed study on the formation of neighboring β-strands during the folding of a monomeric integral membrane protein of the β-barrel type. β-Strand and β-barrel formations were investigated for the eight-stranded transmembrane domain of outer membrane protein A (OmpA) with single-tryptophan (W), single-cysteine (C) OmpA mutants. Based on the OmpA structure, W and C were introduced in two neighboring...

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 Fluorescence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Lipid Bilayers

Share to Protein Folding

Share to Spectrometry, Fluorescence

Share to Spin Labels

Share to Tryptophan

Source

Identifiers

PMID: 21256134
DOI: 10.1016/j.jmb.2011.01.021

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Association of neighboring β-strands of outer membrane protein A in lipid bilayers revealed by site-directed fluorescence quenching.PMID 21256134Read ↗

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

Phi-analysis of the folding of the B domain of protein A using multiple optical probes.Semantic proximity Read ↗

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.Semantic proximity Read ↗

An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Semantic proximity Read ↗

Monitoring the assembly of a secreted bacterial virulence factor using site-specific crosslinking.Semantic proximity Read ↗

Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins.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 ↗

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

A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein.Semantic proximity Read ↗

Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes.Semantic proximity Read ↗

Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.Semantic proximity Read ↗

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

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