Physicochemical Characteristics of a Variant of Chaperon GroEL Apical Domain Designed to Enhance the Expression and Stability of Target Proteins
Author:
Publisher
Pleiades Publishing Ltd
Subject
Applied Microbiology and Biotechnology,Biochemistry
Link
http://link.springer.com/content/pdf/10.1134/S0003683819080088.pdf
Reference19 articles.
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2. Sharapova, O.A., Yurkova, M.S., Laurinavichyute, D.K., et al., Efficient refolding of a hydrophobic protein with multiple S– bonds by on-resin immobilized metal affinity chromatography, J. Chromatogr., 2011, vol. 1218, no. 31, pp. 5115–5119. https://doi.org/10.1016/j.chroma.2011.05.075
3. Fedorov, A.N. and Yurkova, M.S., Molecular Chaperone GroEL—toward a nano toolkit in protein engineering, production and pharmacy, NanoWorld J., 2018, vol. 4, pp. 8–15. https://doi.org/10.17756/nwj.2018-053
4. de Marco, A., Molecular and chemical chaperones for improving the yields of soluble recombinant proteins, Methods Mol. Biol. (Clifton, N.J.), 2011, vol. 705, pp. 31–51. https://doi.org/10.1007/978-1-61737-967-3_3
5. Kapust, R.B. and Waugh, D.S., Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused, Protein Sci. (Publ. Protein Soc.), 1999, vol. 8, no. 8, pp. 1668–1674. https://doi.org/10.1110/ps.8.8.1668
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