Publication: The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli
The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli
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Wall, J. G., & Plückthun, A. (1999). The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli. Protein Engineering, Design & Selection, 12(7), 605–611. https://doi.org/10.1093/protein/12.7.605
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In a systematic study of the periplasmic folding of antibody fragments in Escherichia coli, we have analysed the expression of an aggregation-prone and previously non-functional anti-phosphorylcholine antibody, T15, as a model system and converted it to a functional molecule. Introduction of heavy chain framework mutations previously found to improve the folding of a related antibody led to improved folding of T15 fragments and improved physiology of the host E.coli cells. Manipulation of the complementarity determining regions (CDR)
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Wall, J. G., & Plückthun, A. (1999). The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli. Protein Engineering, Design & Selection, 12(7), 605–611. https://doi.org/10.1093/protein/12.7.605