De novo design of cysteine proteases
Nature, Published online: 14 October 2026; doi:10.1038/s41586-026-11143-w
De novo-designed enzymes use an activated cysteine nucleophile to hydrolyse polypeptide backbones in a sequence-dependent manner.Nature, Published online: 14 October 2026; doi:10.1038/s41586-026-11143-w
De novo-designed enzymes use an activated cysteine nucleophile to hydrolyse polypeptide backbones in a sequence-dependent manner.Nature, Published online: 14 October 2026; doi:10.1038/s41586-026-11167-2
RFdiffusion methods are used to de novo design proteins with water-activating zinc-based active sites adjacent to a peptide substrate binding pocket, yielding highly active, programmable proteases with potential applications in therapeutics, biotechnology and bioremediation.Nature, Published online: 09 June 2026; doi:10.1038/s41586-026-10763-6
Author Correction: De novo design of quasisymmetric two-component protein cages