https://doi.org/10.1140/epje/i2013-13071-6
Regular Article
Small angle neutron scattering for the study of solubilised membrane proteins
19889
Institut de Biologie Structurale (IBS), Univ. Grenoble Alpes, F-38027, Grenoble, France
29889
CEA, DSV, IBS, F-38027, Grenoble, France
39889
CNRS, IBS, F-38027, Grenoble, France
49889
Equipe Chimie Bioorganique et Systèmes Amphiphiles, Université d’Avignon et des Pays de Vaucluse, Avignon, France
59889
Institut des Biomolécules Max Mousseron, UMR 5247 CNRS-Universités Montpellier 1 & 2, F-34095, Montpellier, France
69889
Institute Max Von Laue Paul Langevin, F-38042, Grenoble 9, France
79889
Partnership for Structural Biology, ILL EMBL Deuteration Lab, F-38042, Grenoble 9, France
* e-mail: christine.ebel@ibs.fr
Received:
20
December
2012
Revised:
22
April
2013
Accepted:
16
May
2013
Published online:
16
July
2013
Small angle neutron scattering (SANS) is a powerful technique for investigating association states and conformational changes of biological macromolecules in solution. SANS is of particular interest for the study of the multi-component systems, as membrane protein complexes, for which in vitro characterisation and structure determination are often difficult. This article details the important physical properties of surfactants in view of small angle neutron scattering studies and the interest to deuterate membrane proteins for contrast variation studies. We present strategies for the production of deuterated membrane proteins and methods for quality control. We then review some studies on membrane proteins, and focus on the strategies to overcome the intrinsic difficulty to eliminate homogeneously the detergent or surfactant signal for solubilised membrane proteins, or that of lipids for membrane proteins inserted in liposomes.
Key words: Topical issue: Neutron Biological Physics
© EDP Sciences, SIF, Springer-Verlag Berlin Heidelberg, 2013