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

David J. K. Swainsbury, Stefan Scheidelaar, Rienk van Grondelle, J. Antoinette Killian, Michael R. Jones

Research output: Contribution to journalArticlepeer-review

121 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)11803-11807
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number44
Early online date11 Sep 2014
Publication statusPublished - 27 Oct 2014


  • Detergents
  • Membrane proteins
  • Nanodiscs
  • Reaction centers
  • Styrene maleic acid

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