Detergent-free membrane protein purification

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

Abstract

Membrane proteins are localised within a lipid bilayer; in order to purify them for functional and structural studies the first step must involve solubilising or extracting the protein from these lipids. To date this has been achieved using detergents which disrupt the bilayer and bind to the protein in the transmembrane region. However finding conditions for optimal extraction, without destabilising protein structure is time consuming and expensive. Here we present a recently-developed method using a styrene maleic acid (SMA) co-polymer instead of detergents. The SMA co-polymer extracts membrane proteins in a small disc of lipid bilayer which can be used for affinity chromatography purification, thus enabling the purification of membrane proteins while maintaining their native lipid bilayer environment.
Original languageEnglish
Title of host publicationHeterologous expression of membrane proteins
Subtitle of host publicationmethods and protocols
EditorsIsabelle Mus-Veteau
Edition2nd
ISBN (Electronic)978-1-4939-3637-3
DOIs
Publication statusPublished - 26 Aug 2016

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
Volume1432
ISSN (Print)1064-3745

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  • Cite this

    Rothnie, A. J. (2016). Detergent-free membrane protein purification. In I. Mus-Veteau (Ed.), Heterologous expression of membrane proteins: methods and protocols (2nd ed.). (Methods in Molecular Biology; Vol. 1432). https://doi.org/10.1007/978-1-4939-3637-3