Domain swapping in ribonuclease T1 allows the acquisition of double-stranded activity.

@article{Chen2002DomainSI,
  title={Domain swapping in ribonuclease T1 allows the acquisition of double-stranded activity.},
  author={D Chen and Alan X. Lin},
  journal={Protein engineering},
  year={2002},
  volume={15 12},
  pages={997-1003}
}
A mutant of ribonuclease T1 (RNase T1), denoted RNase Talpha, that is designed to recognize double-stranded ribonucleic acid was created. RNase Talpha carries the structure of RNase T1 except for a part of its loop L3 domain, which has been swapped for a corresponding domain from alpha-sarcin. The RNase Talpha maintains the pleated beta-sheet structure and retains the guanyl-specific ribonuclease activity of the wild-type RNase T1. A steady-state kinetic study on the RNase Talpha-catalyzed… CONTINUE READING
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