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Bacterial Reaction Centers Purified with Styrene Maleic Acid Copolymer Retain Native Membrane Functional Properties and Display Enhanced Stability
Author(s) -
Swainsbury David J. K.,
Scheidelaar Stefan,
van Grondelle Rienk,
Killian J. Antoinette,
Jones Michael R.
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201406412
Subject(s) - copolymer , styrene , membrane , maleic acid , micelle , pulmonary surfactant , chemistry , lipid bilayer , amphiphile , bilayer , integral membrane protein , membrane protein , chemical engineering , combinatorial chemistry , organic chemistry , biochemistry , polymer , aqueous solution , engineering
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.