Antifreeze activity enhancement by site directed mutagenesis on an antifreeze protein from the beetle Rhagium mordax.

@article{Friis2014AntifreezeAE,
  title={Antifreeze activity enhancement by site directed mutagenesis on an antifreeze protein from the beetle Rhagium mordax.},
  author={Dennis Steven Friis and Erlend Kristiansen and Nicolas von Solms and Hans Raml\ov},
  journal={FEBS letters},
  year={2014},
  volume={588 9},
  pages={1767-72}
}
The ice binding motifs of insect antifreeze proteins (AFPs) mainly consist of repetitive TxT motifs aligned on a flat face of the protein. However, these motifs often contain non-threonines that disrupt the TxT pattern. We substituted two such disruptive amino acids located in the ice binding face of an AFP from Rhagium mordax with threonine. Furthermore, a mutant with an extra ice facing TxT motif was constructed. These mutants showed enhanced antifreeze activity compared to the wild type at… CONTINUE READING
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Structural characteristics of a novel antifreeze protein from the longhorn beetle Rhagium inquisitor

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