Fig. 1: Comparison of inter-residue distance distributions obtained by SAXS and predicted by AlphaFold for highly disordered proteins.
From: AlphaFold prediction of structural ensembles of disordered proteins
A–K Results for a set of 11 highly disordered proteins for which both SAXS and NMR diffusion measurements are available36. SAXS-derived inter-residue distance distributions are shown in black, and AlphaFold-predicted average inter-residue distance distributions are shown in blue. The cut-off distance in the AlphaFold predictions is 21.84 Å, so the blue lines stop at this value. For comparison, we report the Kullback–Leibler divergence (DKL) between SAXS and AlphaFold-predicted average inter-residue distance distributions The proteins shown are: ANAC046 (A), A1 (B), ProTα (C), GHR-IDC (D), tau (E), Sic1 (F), DSS1 (G), NHE6cmdd (H), RS (I), Hst5 (J), and α-synuclein (K). L For comparison, we show the results for a folded protein (ubiquitin).
