A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains.
Published version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
De Biasio, Alfredo
Ibáñez de Opakua, Alain
Bostock, Mark J
Nietlispach, Daniel https://orcid.org/0000-0003-4364-9291
Diercks, Tammo
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.
Description
Keywords
Archaeal Proteins, Carotenoids, Halogenation, Lipids, Micelles, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Phosphatidylcholines
Journal Title
Chem Commun (Camb)
Conference Name
Journal ISSN
1359-7345
1364-548X
1364-548X
Volume Title
54
Publisher
Royal Society of Chemistry (RSC)
Publisher DOI
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/G011915/1)
Biotechnology and Biological Sciences Research Council (BB/K01983X/1)
Biotechnology and Biological Sciences Research Council (BB/K01983X/1)