Fig. 4
From: Tau local structure shields an amyloid-forming motif and controls aggregation propensity
Tauopathy mutations drive aggregation propensity. a Schematic of tau RD and the derived peptides representing the minimal structural element around 306VQIVYK311. b WT and mutant peptides were disaggregated, resuspended to 200 µM, and allowed to aggregate in the presence of ThT at room temperature. The WT R2R3 and R1R2 fragment peptides yielded no detectible ThT signal change (less than twofold ratio to background signal) over the course of the experiment (see Supplementary Data 1). ThT signals are shown as average of triplicates with standard deviation, are colored according to mutation and are normalized to the maximum for each condition
