Fig. 3: Synthesis and characterizations of the designed peptide heterodimers.
From: De novo design and directed folding of disulfide-bridged peptide heterodimers
a–e Cartoon representations of design models; Cα traces of NMR ensembles (gray) and cartoon representation of the lowest energy conformer of each NMR ensemble (gray) aligned to the design model (blue slate); HPLC chromatograms showing the dimeric folding of these designed heterodimers (concentration of Cys- and Pen-bearing monomers: 100 and 200 μM respectively; * denotes the oxidized Pen-bearing monomers of hd1‒hd5, which are excess relative to the Cys-bearing monomers in the folding buffers); & a peak containing both the correctly-paired antiparallel heterodimer (hd4) and the undesired parallel heterodimer; # denotes the undesired antiparallel heterodimer. CD spectra of the heterodimers were recorded in water at room temperature. TCEP was added to record CD spectra of the reduced monomers (hd1–hd3). Source data are provided as a Source Data file.
