NMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain Swapping

@inproceedings{Spadaccini2012NMRSO,
  title={NMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain Swapping},
  author={Roberta Spadaccini and Carmine Ercole and Maria Antonietta Gentile and Domenico Sanfelice and Rolf Boelens and Rainer W Wechselberger and Gyula Batta and Andrea Bernini and Neri Niccolai and Delia Picone},
  booktitle={PloS one},
  year={2012}
}
Three-dimensional domain swapping is a common phenomenon in pancreatic-like ribonucleases. In the aggregated state, these proteins acquire new biological functions, including selective cytotoxicity against tumour cells. RNase A is able to dislocate both N- and C-termini, but usually this process requires denaturing conditions. In contrast, bovine seminal ribonuclease (BS-RNase), which is a homo-dimeric protein sharing 80% of sequence identity with RNase A, occurs natively as a mixture of… CONTINUE READING

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