Fig. 3.

Primary structure analyses of mouse prion protein (mPrP). The secondary structural elements determined on the basis of the nuclear magnetic resonance structure (PDB ID 1AG2), octameric repeat, and hydrophobic cluster are shown schematically at the top of the figure. a Hydrophobic profile of mPrP was predicted by the Kyte and Doolittle method (Kyte and Doolittle 1982). The amino acid sequence of mPrP is shown and colored red (helix), green (sheet), or black (random), depending on the secondary structure predicted by the PHD algorithms (Rost et al. 1994). b Prediction of aggregation propensities of mPrP. The β-aggregation propensities predicted by PASTA 2.0 (black) (Walsh et al. 2014) and TANGO (red) (Fernandez-Escamilla et al. 2004) are plotted against the residue number of mPrP. PrP mutations causing inherited human prion disease are shown by solid black circles