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

Published version
Peer-reviewed

Type

Article

Change log

Authors

De Biasio, Alfredo 
Ibáñez de Opakua, Alain 
Bostock, Mark J 
Nietlispach, Daniel  ORCID logo  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

Volume Title

54

Publisher

Royal Society of Chemistry (RSC)
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/G011915/1)
Biotechnology and Biological Sciences Research Council (BB/K01983X/1)