Triosephosphate isomerase by consensus design: dramatic differences in physical properties and activity of related variants.

@article{Sullivan2011TriosephosphateIB,
  title={Triosephosphate isomerase by consensus design: dramatic differences in physical properties and activity of related variants.},
  author={Brandon J Sullivan and Venuka Durani and Thomas J. Magliery},
  journal={Journal of molecular biology},
  year={2011},
  volume={413 1},
  pages={195-208}
}
Consensus design, the selection of mutations based on the most common amino acid in each position of a multiple sequence alignment, has proven to be an efficient way to engineer stabilized mutants and even to design entire proteins. However, its application has been limited to small motifs or small families of highly related proteins. Also, we have little idea of how information that specifies a protein's properties is distributed between positional effects (consensus) and interactions between… CONTINUE READING
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