Strategies for protein coexpression in Escherichia coli
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology,Biochemistry,Biotechnology
Link
http://www.nature.com/articles/nmeth0106-55.pdf
Reference12 articles.
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3. Bross, P. et al. Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli–expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation. Biochim. Biophys. Acta 1182, 264–274 (1993).
4. Woestenenk, E.A., Hammarstrom, M., van den Berg, S., Hard, T. & Berglund, H. His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors. J. Struct. Funct. Genomics 5, 217–229 (2004).
5. Kapust, R.B. & Waugh, D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8, 1668–1674 (1999).
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