Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold.

@article{Lehti2000AlphaamylaseIS,
  title={Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold.},
  author={Janne Lehti{\"o} and Tuula T. Teeri and Per Ake Nygren},
  journal={Proteins},
  year={2000},
  volume={41 3},
  pages={
          316-22
        }
}
A disulfide bridge-constrained cellulose binding domain (CBD(WT)) derived from the cellobiohydrolase Cel7A from Trichoderma reesei has been investigated for use in scaffold engineering to obtain novel binding proteins. The gene encoding the wild-type 36 aa CBD(WT) domain was first inserted into a phagemid vector and shown to be functionally displayed on M13 filamentous phage as a protein III fusion protein with retained cellulose binding activity. A combinatorial library comprising 46 million… CONTINUE READING

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