Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 beta-lactamase.

@article{Simm2007InvestigatingPS,
  title={Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 beta-lactamase.},
  author={Alan M. Simm and Amy J. Baldwin and Kathy Busse and D Dafydd Jones},
  journal={FEBS letters},
  year={2007},
  volume={581 21},
  pages={3904-8}
}
While the deletion of an amino acid is a common mutation observed in nature, it is generally thought to be disruptive to protein structure. Using a directed evolution approach, we find that the enzyme TEM-1 beta-lactamase was broadly tolerant to the deletion mutations sampled. Circa 73% of the variants analysed retained activity towards ampicillin, with deletion mutations observed in helices and strands as well as regions important for structure and function. Several deletion variants had… CONTINUE READING

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