Fig. 2
From: Tau local structure shields an amyloid-forming motif and controls aggregation propensity
Tau RD encodes global and local structure. a Cartoon schematic of tau RD used for XL-MS studies colored according to repeat domain. Recombinant WT and P301L tau RD were heated at 37 °C, 50 °C or 75 °C for 1 hour, then chemically cross-linked using DSS. After cross-linking, trypsin fragmentation, and LC-MS/MS analysis were performed. Each sample was carried out in five technical replicates. b Total consensus cross-links parsed by temperature and location in WT and P301L tau RD: within N-terminus (blue; residues 243–310; N-term), within C-terminus (orange; residues 311–380; C-term), span N- and C-terminus (magenta; between residues 243–310 and 311–380; N-C) and between repeat 2 and repeat 3 (R2R3) (gray; between residues 275–305 and 306–336). c–e Consensus cross-links (circles) are shown in contact maps color coded by average frequency across replicates. The theoretical lysine pairs are shown in the background as gray circles. Cross-link contacts within the N-term (blue), C-term (red), and across N- to C-term (purple) are shown as sectors. The x and y axis are colored according to repeat number as in Fig. 1. The dashed boxes define inter-repeat cross-links observed between repeat 2 and repeat 3. f–h Same as c–e above, except with tau RD that contains a P301L mutation
