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


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.

SUBMITTER: Swainsbury DJ 

PROVIDER: S-EPMC4271668 | BioStudies | 2014-01-01T00:00:00Z

REPOSITORIES: biostudies

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