BETASCAN output for amyloid and prion proteins with experimentally determined β-structures.

Green vertical brackets indicate experimentally derived locations of β-strands; blue brackets indicate locations determined by a separate method. In the same manner as Figure 1b, BETASCAN predictions are marked as horizontal lines, shading from red (maximum predicted score) to yellow (zero score, i.e., probability equal to background). Overlapping lines indicate alternate folding patterns for the β-strands, with indicated probability. Two graphs are included to display the results for each orientation of the strand. For purposes of comparison, the set of highest-scoring non-overlapping strands in the BETASCAN single-strand prediction was taken as the predicted structure. Corresponding outputs of PASTA [49],[50], TANGO [45], and Zyggregator [46] are displayed below the BETASCAN results. Refer to Table 1 for a summary of the correspondences of these predictions. (A) amyloid-β structure as determined by Luehrs et al. [18] (green) and Petkova et al. [19] (blue); (B) het-S structure as determined by Ritter et al. [20] (green) and Wasmer et al. [21] (blue); (C) α-synuclein structure as determined by Heise et al. [51]; (D) amylin structure as determined by Kajava et al. [53]; (E) tau protein fragment PHF43 structure as determined by von Bargen et al. [52].