Fig. 2: Biophysical characterization of designed protein–peptide complexes.
From: De novo design of modular peptide-binding proteins by superhelical matching
a, Computational models of the designed six-repeat version of protein–peptide complexes. Designed proteins are shown in cartoons and peptides in sticks. b, Magnified views for single designed protein–peptide interaction units. Residues interacting across the interface are shown in sticks. c, Predicted SAXS profiles overlaid on experimental SAXS data points. The scattering vector q is on the x axis (from 0 to 0.25) and the intensity (I) is on the y axis on a logarithmic scale. AU, arbitrary units. d, Circular dichroism (CD) spectra at different temperatures (blue, 20 °C; orange, 95 °C; green, 95 °C followed by 20 °C). e, Bio-layer interferometry characterization of the binding of designed proteins to the corresponding peptide targets. Twofold serial dilutions were tested for each binder and the highest concentration is labelled. The biotinylated target peptides were loaded onto streptavidin biosensors, and incubated with designed binders in solution to measure association and dissociation.
