A generalized approach for NMR studies of lipid–protein interactions based on sparse fluorination of acyl chains
2018
De BiasioPresent address: Department of Molecular and Cell Biology, Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK. E-mail: [email protected] authors contributed equally. Alfredo | Ibáñez de Opakua, Alain | Bostock, Mark J. | Nietlispach, Daniel | Diercks, Tammo | Blanco, Francisco J.
Sparse lipid fluorination enhances the lipids' ¹H signal dispersion, enables clean molecular distinction by ¹⁹F NMR, and evinces micelle insertion of proteins via fluorine-induced signal shifts. We present a minimal fluorination scheme, and illustrate the concept on di-(4-fluoro)-heptanoylphosphatidylcholine micelles and solubilised seven-helix transmembrane pSRII protein.
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