ArticleJournal of biomolecular NMR2011
Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Pathological mutations in the phospholamban cytoplasmic region affect its topology and dynamics modulating the extent of SERCA inhibition.Biochimica et biophysica acta. Biomembranes · 2024Article
- Factors Influencing Green Purchase Intention: Moderating Role of Green Brand Knowledge.International journal of environmental research and public health · 2021Article
- Sensitivity enhancement for membrane proteins reconstituted in parallel and perpendicular oriented bicelles obtained by using repetitive cross-polarization and membrane-incorporated free radicals.Journal of biomolecular NMR · 2017Article
- Optimal Bicelle Size q for Solution NMR Studies of the Protein Transmembrane Partition.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.Nature communications · 2014Article
- Solution NMR studies on the orientation of membrane-bound peptides and proteins by paramagnetic probes.Molecules (Basel, Switzerland) · 2013Review
- Determining the depth of insertion of dynamically invisible membrane peptides by gel-phase ¹H spin diffusion heteronuclear correlation NMR.Journal of biomolecular NMR · 2013Article
- On the role of NMR spectroscopy for characterization of antimicrobial peptides.Methods in molecular biology (Clifton, N.J.) · 2013Review
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Authors and funding
4 authors.
Funding
Abstract
In studies of membrane proteins, knowledge of protein topology can provide useful insight into both structure and function. In this work, we present a solution NMR method for the measurement the tilt angle and average immersion depth of alpha helices in membrane proteins, from analysis of the paramagnetic relaxation rate enhancements arising from dissolved oxygen. No modification to the micelle or protein is necessary, and the topology of both transmembrane and amphipathic helices are readily determined. We apply this method to the measure the topology of a monomeric mutant of phospholamban (AFA-PLN), a 52-residue membrane protein containing both an amphipathic and a transmembrane alpha helix. In dodecylphosphocholine micelles, the amphipathic helix of AFA-PLN was found to have a tilt angle of 87° ± 1° and an average immersion depth of 13.2 Å. The transmembrane helix was found to have an average immersion depth of 5.4 Å, indicating residues 41 and 42 are closest to the micelle centre. The resolution of paramagnetic relaxation rate enhancements from dissolved oxygen compares favourably to those from Ni (II), a hydrophilic paramagnetic species.
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