PMID:21992454

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Citation

Platas, G, Rodríguez-Carmona, E, García-Fruitós, E, Cano-Garrido, O and Villaverde, A (2011) Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control. Microb. Cell Fact. 10:79

Abstract

The effects and effectiveness of the chaperone pair GroELS on the yield and quality of recombinant polypeptides produced in Escherichia coli are matter of controversy, as the reported activities of this complex are not always consistent and eventually indicate undesired side effects. The divergence in the reported data could be due, at least partially, to different experimental conditions in independent research approaches.

Links

PubMed PMC3207889 Online version:10.1186/1475-2859-10-79

Keywords

Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Green Fluorescent Proteins/chemistry; Green Fluorescent Proteins/genetics; Green Fluorescent Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Hot Temperature; Protein Conformation; Protein Folding; beta-Galactosidase/chemistry; beta-Galactosidase/genetics; beta-Galactosidase/metabolism

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