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A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains
Journal article   Open access  Peer reviewed

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

Alfredo De Biasio, Alain Ibanez de Opakua, Mark J. Bostock, Daniel Nietlispach, Tammo Diercks and Francisco J. Blanco
Chemical communications (Cambridge, England), Vol.54(53), pp.7306-7309
2018
DOI: https://doi.org/10.1039/c8cc02483a
PMID: 29905339

Abstract

Chemistry Chemistry, Multidisciplinary Physical Sciences Science & Technology
Sparse lipid fluorination enhances the lipids' H-1 signal dispersion, enables clean molecular distinction by F-19 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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https://doi.org/10.1039/c8cc02483aView
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