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Nucleic Acids Research 2006 34(Database Issue):D207-D212; doi:10.1093/nar/gkj080
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Nucleic Acids Research, 2006, Vol. 34, Database issue D207-D212
© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org


Article

The REFOLD database: a tool for the optimization of protein expression and refolding

Michelle K. M. Chow1, Abdullah A. Amin1,2, Kate F. Fulton1, Thushan Fernando4, Lawrence Kamau4, Chris Batty4, Michael Louca4, Storm Ho4, James C. Whisstock1,2,3, Stephen P. Bottomley1,* and Ashley M. Buckle1,2,*

1Department of Biochemistry and Molecular Biology PO Box 13D Monash University Victoria 3800 Australia 2Victorian Bioinformatics Consortium PO Box 53 Monash University Clayton, Victoria, 3800, Australia 3ARC Centre for Structure and Functional Microbial Genomics, Monash University Clayton, Victoria 3800, Australia 4Swinburne University of Technology Hawthorn Campus, Victoria, 3136, Australia

*To whom correspondence should be addressed. Tel: +613 9905 3781; Email: ashley.buckle{at}med.monash.edu.au

Received August 10, 2005. Revised October 11, 2005. Accepted October 11, 2005.

A large proportion of proteins expressed in Escherichia coli form inclusion bodies and thus require renaturation to attain a functional conformation for analysis. In this process, identifying and optimizing the refolding conditions and methodology is often rate limiting. In order to address this problem, we have developed REFOLD, a web-accessible relational database containing the published methods employed in the refolding of recombinant proteins. Currently, REFOLD contains >300 entries, which are heavily annotated such that the database can be searched via multiple parameters. We anticipate that REFOLD will continue to grow and eventually become a powerful tool for the optimization of protein renaturation. REFOLD is freely available at http://refold.med.monash.edu.au.


Correspondence may also be addressed to Stephen P. Bottomley. Tel: +613 9905 4699; Email: steve.bottomley{at}med.monash.edu.au


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