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Protecting role of cosolvents in protein denaturation by SDS: a structural study by Catherine Michaux; Jenny Pouyez; Johan Wouters; Gilbert G Privé is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Background Recently, we reported a unique approach to preserve the activity of some proteins in the presence of the denaturing agent, Sodium Dodecyl Sulfate (SDS). This was made possible by addition of the amphipathic solvent 2,4-Methyl-2-PentaneDiol (MPD), used as protecting but also as refolding agent for these proteins. Although the persistence of the protein activity in the SDS/MPD mixture was clearly established, preservation of their structure was only speculative until now. ## Results In this paper, a detailed X-ray study addresses the pending question. Crystals of hen egg-white lysozyme were grown for the first time in the presence of MPD and denaturing concentrations of SDS. Depending on crystallization conditions, tetragonal crystals in complex with either SDS or MPD were collected. The conformation of both structures was very similar to the native lysozyme and the obtained complexes of SDS-lysozyme and MPD-lysozyme give some insights in the interplay of protein-SDS and protein-MPD interactions. ## Conclusion This study clearly established the preservation of the enzyme structure in a SDS/MPD mixture. It is hypothesized that high concentrations of MPD would change the

Who reads Protecting role of cosolvents in protein denaturation by SDS: a structural study?

Author

Catherine Michaux; Jenny Pouyez; Johan Wouters; Gilbert G Privé

Publisher

BioMed Central; Springer (Biomed Central Ltd.); London: BioMed Central, 2001-; Springer Science and Business Media LLC (ISSN 1472-6807)

Published

2008

Language

EN

ISBN

9781472680785

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)