A single amino acid substitution can restore the solubility of aggregated colicin A mutants in Escherichia coli.

@article{Izard1994ASA,
  title={A single amino acid substitution can restore the solubility of aggregated colicin A mutants in Escherichia coli.},
  author={Jacques Y. Izard and Michael W Parker and Martine Chartier and Denis Duch{\'e} and Daniel Baty},
  journal={Protein engineering},
  year={1994},
  volume={7 12},
  pages={1495-500}
}
Mutants of colicin A have been prepared in which the three tryptophan residues (Trp86, Trp130 and Trp140), localized in the C-terminal domain of the soluble wild-type protein, have been substituted by phenylalanine. The Trp140Phe single mutation had the effect of decreasing the percentage of protein that is expressed as insoluble aggregates. The created hydrophobic cavity decreased the stability of the protein during its folding, resulting in partial aggregation in the cytoplasm of the… CONTINUE READING