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

Unfolding study of a trimeric membrane protein AcrB.

Protein science : a publication of the Protein Society - 1 Jul 2014

Ye Cui, Wang Zhaoshuai, Lu Wei, Wei Yinan

Abstract excerpt

The folding of a multi-domain trimeric α-helical membrane protein, Escherichia coli inner membrane protein AcrB, was investigated. AcrB contains both a transmembrane domain and a large periplasmic domain. Protein unfolding in sodium dodecyl sulfate (SDS) and urea was monitored using the intrinsic fluorescence and circular dichroism spectroscopy. The SDS denaturation curve displayed a sigmoidal profile, which...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Multidrug Resistance-Associated Proteins
Share to Phenylalanine

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

Share to Protein Denaturation

Share to Protein Multimerization

Share to Sodium Dodecyl Sulfate

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 24715637
DOI: 10.1002/pro.2471
PMCID: PMC4088973

Genes

SDS

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

Unfolding study of a trimeric membrane protein AcrB.PMID 24715637Read ↗

AcrB trimer stability and efflux activity, insight from mutagenesis studies.Semantic proximity Read ↗

Role of a conserved residue R780 in Escherichia coli multidrug transporter AcrB.Semantic proximity Read ↗

Dissecting the function of a protruding loop in AcrB trimerization.Semantic proximity Read ↗

Annexin B12 Trimer Formation is Governed by a Network of Protein-Protein and Protein-Lipid Interactions.Semantic proximity Read ↗

Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy.Semantic proximity Read ↗

Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli.Semantic proximity Read ↗

Functional relevance of AcrB Trimerization in pump assembly and substrate binding.Semantic proximity Read ↗

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

Increased stability upon heptamerization of the pore-forming toxin aerolysin.Semantic proximity Read ↗

Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain.Semantic proximity Read ↗

Unfolding mechanics of multiple OspA substructures investigated with single molecule force spectroscopy.Semantic proximity Read ↗

Structural stability of GlcV, the nucleotide binding domain of the glucose ABC transporter of Sulfolobus solfataricus.Semantic proximity Read ↗

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