Extended Data Fig. 9: Residue frequencies in beta-sheets and LARKS.
a. The relative frequencies in which each amino acid is observed in beta-sheets (bar graph). Analysis of the disease-related mutations predicted to convert LARKS to zippers shows little correlation of residues mutating to more beta-sheet prone amino acids compared to wild-type (insert). b. Comparison of relative amino acid frequencies between all experimentally determined structures of LARKS versus amyloid fibrils (bar graph). There is a drastically higher enrichment of glycines in LARKS compared to canonical amyloid structures, likely contributing to their kinked structures. Pathogenic mutations predicted to convert LARKS to steric zippers lead to a transition from residues enriched in LARKS to those that are not. Data for graphs is available as source data.
