Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent
AuthorSwarbrick, JD; Karas, JA; Li, J; Velkov, T
Source TitleChemical Communications
PublisherRoyal Society of Chemistry
AffiliationSchool of Chemistry
Pharmacology and Therapeutics
Biochemistry and Molecular Biology
Document TypeJournal Article
CitationsSwarbrick, J. D., Karas, J. A., Li, J. & Velkov, T. (2020). Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent. Chemical Communications, 56 (19), pp.2897-2900. https://doi.org/10.1039/c9cc09207b.
Access StatusThis item is currently not available from this repository
[Tm(DPA)3]3- was used to generate multiple, paramagnetic nuclear Overhauser effect NMR spectra of cationic peptides when weakly bound to a lipopolysaccharide micelle. Increased spectral resolution combined with a marked increase in the number of distance restraints yielded high resolution structures of polymyxin and MSI-594 in the liposaccharide bound state.
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