Fig. 4: Orthogonality of peptide heterodimerizations.
From: De novo design and directed folding of disulfide-bridged peptide heterodimers
a Excellent orthogonality was observed between each two heterodimers except for the orthogonality between hd1 and hd2 (Supplementary Figs. 27‒32). b and c Excellent orthogonality was observed in the formation of three heterodimers (b: hd1/hd3/hd4; c: hd2/hd3/hd4). m1‒m4 denote the oxidized products of the excess Pen-bearing monomers of hd1‒hd4, respectively. d and e Oxidation-induced dimerization leading to formation of the tandem heterodimers: hd1 and hd3 were connected with a flexible linker containing a tobacco etch virus (TEV) protease cleavage site (ENLYFQG). Source data are provided as a Source Data file.
