De novo designed cysteine proteases cut peptide bonds at chosen sequences using folds unlike natural enzymes
Researchers at the University of Washington's Institute for Protein Design, with collaborators at ETH Zurich, KAIST, Stanford University, the University of Oxford, the University of Cambridge and Lawrence Berkeley National Laboratory, reported in Nature, published online on 14 October, the de novo computational design of enzymes that hydrolyse the peptide backbone using an activated cysteine nucleophile.