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

MAS solid-state NMR studies on the multidrug transporter EmrE.

Biochimica et biophysica acta - 1 Dec 2007

Agarwal Vipin, Fink Uwe, Schuldiner Shimon, Reif Bernd

Abstract excerpt

We study the uniformly 13C,15N isotopically enriched Escherichia coli multidrug resistance transporter EmrE using MAS solid-state NMR. Solid-state NMR can provide complementary structural information as the method allows studying membrane proteins in their native environment as no detergent is re...

Read the complete abstract on PubMed

Topics

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

Share to Antiporters
Share to Carbon Isotopes
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Membrane Proteins

Share to Microscopy, Electron

Share to Nitrogen Isotopes

Share to Organophosphorus Compounds

Source

Identifiers

PMID: 17976529
DOI: 10.1016/j.bbamem.2007.09.012

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-17976529-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

MAS solid-state NMR studies on the multidrug transporter EmrE.PMID 17976529Read ↗

The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.Semantic proximity Read ↗

Protonation of a glutamate residue modulates the dynamics of the drug transporter EmrE.Semantic proximity Read ↗

Protocols for Studying the Interaction of MSI-78 with the Membranes of Whole Gram-Positive and Gram-Negative Bacteria by NMR.Semantic proximity Read ↗

An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli.Semantic proximity Read ↗

Anti-parallel membrane topology of a homo-dimeric multidrug transporter, EmrE.Semantic proximity Read ↗

Inducing conformational preference of the membrane protein transporter EmrE through conservative mutationsSemantic proximity Read ↗

Probing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site-directed spin labeling approach.Semantic proximity Read ↗

Structure analysis of the fourth transmembrane domain of Nramp1 in model membranes.Semantic proximity Read ↗

Sparse Labeling PELDOR Spectroscopy on Multimeric Mechanosensitive Membrane Channels.Semantic proximity Read ↗

Solid-state NMR analysis of the sodium pump Krokinobacter rhodopsin 2 and its H30A mutant.Semantic proximity Read ↗

Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR.Semantic proximity Read ↗

Probing the ATP hydrolysis cycle of the ABC multidrug transporter LmrA by pulsed EPR spectroscopy.Semantic proximity Read ↗

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