Fig. 3
From: Tau local structure shields an amyloid-forming motif and controls aggregation propensity
Wild-type and mutant peptides differentially populate collapsed and extended conformations. a Trimer conformations obtained from MD simulations of WT peptide fragment (R2R3-WT) with the sequence 295DNIKHVPGGGSVQIVYK311. Two-dimensional root mean-squared-differences (RMSD’s) are calculated between all pairs of conformations visited during MD simulations. Snapshots of trimeric structures are depicted for selected metastable basins, with each peptide monomer represented by a different color. b The same analysis as in a, but for the P301L substituted trimer. c The free-energy surface as a function of deviation from a canonical hairpin structure. Two distinct basins, corresponding to collapsed and extended sub-ensembles, are found in WT and P301L peptide fragment, respectively. Error bars represent a 95% CI of each RMSD bin
