The expression and harvesting of proteins from insoluble inclusion bodies by solubilization and refolding is a technique commonly used in the production of recombinant proteins. Despite the importance of refolding, publications in the literature are essentially ad hoc reports consisting of a dazzling array of experimental protocols and a diverse collection of buffer cocktails. For the protein scientists, using this information to refold their protein of interest presents enormous challenges. Here, we describe some of the practical considerations in refolding and present several standard protocols. Further, we describe how refolding procedures can be designed and modified using the information in the REFOLD database (http://refold.med.monash.edu.au), a freely available, open repository for protocols describing the refolding and purification of recombinant proteins. © 2011 Springer Science+Business Media, LLC.
|Title of host publication||Protein folding, misfolding, and disease|
|Subtitle of host publication||Methods and protocols|
|Editors||Andrew F. Hill, Kevin J. Barnham, Stephen P. Bottomley, Roberto Cappai|
|Number of pages||13|
|Publication status||Published - 2011|
|Name||Methods in Molecular Biology|
Phan, J., Yamout, N., Schmidberger, J., Bottomley, S. P. P., & Buckle, A. M. M. (2011). Refolding your protein with a little help from REFOLD. In A. F. Hill, K. J. Barnham, S. P. Bottomley, & R. Cappai (Eds.), Protein folding, misfolding, and disease: Methods and protocols (Vol. 752, pp. 45-57). (Methods in Molecular Biology). Humana Press. https://doi.org/10.1007/978-1-60327-223-0_4