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Angew Chem Int Ed Engl. 2014 Oct 27;53(44):11803-7. doi: 10.1002/anie.201406412. Epub 2014 Sep 11.

Bacterial reaction centers purified with styrene maleic acid copolymer retain native membrane functional properties and display enhanced stability.

Author information

1
School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD (UK).

Abstract

Integral membrane proteins often present daunting challenges for biophysical characterization, a fundamental issue being how to select a surfactant that will optimally preserve the individual structure and functional properties of a given membrane protein. Bacterial reaction centers offer a rare opportunity to compare the properties of an integral membrane protein in different artificial lipid/surfactant environments with those in the native bilayer. Here, we demonstrate that reaction centers purified using a styrene maleic acid copolymer remain associated with a complement of native lipids and do not display the modified functional properties that typically result from detergent solubilization. Direct comparisons show that reaction centers are more stable in this copolymer/lipid environment than in a detergent micelle or even in the native membrane, suggesting a promising new route to exploitation of such photovoltaic integral membrane proteins in device applications.

KEYWORDS:

detergents; membrane proteins; nanodiscs; reaction centers; styrene maleic acid

PMID:
25212490
PMCID:
PMC4271668
DOI:
10.1002/anie.201406412
[Indexed for MEDLINE]
Free PMC Article

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