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Issue 53, 2018
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A generalized approach for NMR studies of lipid–protein interactions based on sparse fluorination of acyl chains

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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.

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

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Supplementary files

Article information


Submitted
27 Mar 2018
Accepted
21 May 2018
First published
15 Jun 2018

This article is Open Access

Chem. Commun., 2018,54, 7306-7309
Article type
Communication

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

A. De Biasio, A. Ibáñez de Opakua, M. J. Bostock, D. Nietlispach, T. Diercks and F. J. Blanco, Chem. Commun., 2018, 54, 7306
DOI: 10.1039/C8CC02483A

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