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.
Bacterial Reaction Centers Purified with Styrene Maleic Acid Copolymer Retain Native Membrane Functional Properties and Display Enhanced Stability**
D. Swainsbury,S. Scheidelaar,Rienk van Grondelle,J. Killian,Michael R. Jones
Published 2014 in Angewandte Chemie
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PUBLICATION RECORD
- Publication year
2014
- Venue
Angewandte Chemie
- Publication date
2014-09-11
- Fields of study
Biology, Medicine, Materials Science, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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