A generalized approach for NMR studies of lipid–protein interactions based on sparse fluorination of acyl chains

Abstract

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.