ArticleProtein science : a publication of the Protein Society2012
Identification and removal of nitroxide spin label contaminant: impact on PRE studies of α-helical membrane proteins in detergent.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Optimization of Detergent-Mediated Reconstitution of Influenza A M2 Protein into Proteoliposomes.Membranes · 2018Article
- Mapping membrane protein backbone dynamics: a comparison of site-directed spin labeling with NMR 15N-relaxation measurements.Biophysical journal · 2014Article
- Backbone ¹H, ¹³C and ¹⁵N resonance assignments of the α-helical membrane protein TM0026 from Thermotoga maritima.Biomolecular NMR assignments · 2013Article
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2 authors.
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Abstract
NMR paramagnetic relaxation enhancement (PRE) provides long-range distance constraints (~15-25 Å) that can be critical to determining overall protein topology, especially where long-range NOE information is unavailable such as in the case of larger proteins that require deuteration. However, several challenges currently limit the use of NMR PRE for α-helical membrane proteins. One challenge is the nonspecific association of the nitroxide spin label to the protein-detergent complex that can result in spurious PRE derived distance restraints. The effect of the nitroxide spin label contaminant is evaluated and quantified and a robust method for the removal of the contaminant is provided to advance the application of PRE restraints to membrane protein NMR structure determination.
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