Extended Data Fig. 6: Diffusing de novo binder design to prion protein.
From: Diffusing protein binders to intrinsically disordered proteins
a, Jpred4 prediction for the prion target region, outlined by a dashed box, shows a β-strand prediction for five residues. b,g, Circular dichroism data show that the PRI28 binder (g) and IL-2RG-30 (g) has helical secondary structure and is stable up to 95 °C. c, The design model of PRI22, designed using target sequence information alone. d, The BLI data revealed that the binding affinity of PRI22 is 1.88 μM (left), which improved to 80 nM after two-sided partial diffusion (right). e, The specificity test for prion binder PRI28 (Fig. 2i) against various amyloid target sequences showed that PRI28 is highly specific, with some cross-reactivity observed only with TEME106B. f, Jpred4 secondary structure prediction for the IL-2RG target region, with the designed sequence highlighted by a black dashed box. Within this region, a short β-strand (green) is predicted for five residues, indicating localized strand propensity.
