Fig. 2: Design principle for structurally ordered peptide heterodimers. | Nature Communications

Fig. 2: Design principle for structurally ordered peptide heterodimers.

From: De novo design and directed folding of disulfide-bridged peptide heterodimers

Fig. 2

a Typical workflow of designing peptide heterodimers from disulfide-rich mini-proteins (e.g., from 1kv0 to hd1). b Designed heterodimers (hd2‒hd5) crosslinked through 2‒4 interchain disulfide bonds. Sequences of these peptides were given in Supplementary Table 1. c Schematic representation of the RPX method for the identification and placement of disulfides within protein/peptide scaffolds. PDB output files for these designed peptides are provided in a Supplementary file.

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