Structure of micelle bound cationic peptides by NMR spectroscopy using a lanthanide shift reagent
| Autor: | Jian Li, James D. Swarbrick, John A. Karas, Tony Velkov |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Lanthanide
Protein Conformation Chemistry Ligand Metals and Alloys Cationic polymerization General Chemistry Nuclear magnetic resonance spectroscopy Nuclear Overhauser effect Lanthanoid Series Elements Micelle Catalysis Surfaces Coatings and Films Electronic Optical and Magnetic Materials NMR spectra database Crystallography Reagent Materials Chemistry Ceramics and Composites Indicators and Reagents Peptides Nuclear Magnetic Resonance Biomolecular Micelles Antimicrobial Cationic Peptides Polymyxin B |
| Zdroj: | Chemical Communications. 56:2897-2900 |
| ISSN: | 1364-548X 1359-7345 |
| DOI: | 10.1039/c9cc09207b |
| Popis: | [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. |
| Databáze: | OpenAIRE |
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