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Guillaume Roussel, Eric A. Perpète, André Matagne, Emmanuel Tinti and Catherine Michaux Towards a universal method for protein refolding: The trimeric beta barrel membrane Omp2a as a test case Biotechnology and Bioengineering 110

Version of Record online: 18 SEP 2012 | DOI: 10.1002/bit.24722

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The structural determination of membrane proteins is still a huge challenge in structural biology, as it is often difficult to isolate them in a native form. There is an urgent need to set up efficient refolding processes to circumvent such a problem. This contribution describes how a method, based on the association of a detergent (SDS) and 2-methyl-2,4-pentanediol (MPD) was able to refold a trimeric membrane protein. The efficiency of our technique is demonstrated and the results also confirm its transferability.

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