A generalized approach for NMR studies of lipid–protein interactions based on sparse fluorination of acyl chains-Reference-Cited by-同舟云学术

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

Published:2018 Issue:53 Volume:54 Page:7306-7309
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

De Biasio Alfredo¹²³^ORCID,Ibáñez de Opakua Alain¹²³,Bostock Mark J.⁴⁵⁶⁷^ORCID,Nietlispach Daniel⁴⁵⁶⁷^ORCID,Diercks Tammo¹²³^ORCID,Blanco Francisco J.¹²³⁸⁹^ORCID

Affiliation:

1. CIC bioGUNE

2. Derio

3. Spain

4. Department of Biochemistry

5. University of Cambridge

6. Cambridge

7. UK

8. IKERBASQUE

9. Basque Foundation for Science

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.

Funder

Ministerio de Economía y Competitividad

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C8CC02483A

Reference19 articles.

1. How Membranes Shape Protein Structure

2. The changing landscape of membrane protein structural biology through developments in electron microscopy

3. The measurement of immersion depth and topology of membrane proteins by solution state NMR

4. Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy

5. Current applications of 19F NMR to studies of protein structure and dynamics

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