Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology
Link
http://www.nature.com/articles/nprot.2007.400.pdf
Reference22 articles.
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3. Houry, W.A., Frishman, D., Eckerkorn, C., Lottspeich, F. & Hartl, F.U. Identification of in vivo substrates of the chaperonin GroEL. Nature 402, 147–154 (1999).
4. Veinger, L., Diamant, S., Buchner, J. & Goloubinoff, P. The small heat shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273, 11032–11037 (1998).
5. Goloubinoff, P., Mogk, A., Ben Zvi, A.P., Tomoyasu, T. & Bukau, B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Procl. Natl. Acad. Sci. USA 96, 13732–13737 (1999).
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