An original surfactant-based protein refolding method
Major issues in biochemistry include mastering the denatured proteins refolding and understanding the mechanisms. The refolding step is often an inefficient empirical process, time and resources-consuming. The development of new refolding techniques is therefore urgently awaited. In that context, we have successfully shown the reliability of a new procedure based on the association of Sodium Dodecyl Sulfate (SDS) and 2-Methyl-2,4-pentanediol (MPD). To our knowledge, this is the only protocol described proved to efficiently refold several types of proteins. The goal of the project is to understand the molecular basis of the particular assembly and highlight its relevance in the refolding process. Deeper analyses are requested to determine the influence on the specific interactions and complex stability of parameters such as SDS/MPD concentrations, pH, ionic strength and temperature. SANS is the perfect technique to investigate the micelle structure, micelle-solvent interactions and structural changes upon self-aggregation. We shall also investigate the refolding of a model protein, i.e. lysozyme, and give some insights in the interplay of protein-SDS and protein-MPD interactions.
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MICHAUX Catherine; E.A. Perpète and PORCAR Lionel. (2018). An original surfactant-based protein refolding method. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-782
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