Comparison of the local structural stabilities of mammalian prion protein (PrP) by fragment molecular orbital calculations

Figures & data

Figure 1. Amino acid sequences of C-terminal region of 6 mammalian prion proteins (PrPs). The 6 mammalian PrP sequences were compared. The bold residues are not conserved among the 6 PrPs. The residue numbering for all PrP was aligned with that for human PrP. The secondary structural element information was shown as α for α–helix, β for β–strand and L for loop or coil region.

Figure 2. Superposition of the nuclear magnetic resonance (NMR) structures of 6 mammalian PrPs. The structures of backbone (A) and side chains (B) are illustrated: human (red), bovine (green), mouse (blue), hamster (purple), dog (yellow) and cat (orange).

Table 1. The pair interaction energies (ΔE^Pair) of 6 mammalian PrP models under neutral pH condition

Figure 3. First principal component scores in the principal component analysis (PCA) for the ΔE^Pair of mammalian PrP. The scores under neutral (pH 7.0) and mildly acidic (pH 4.5) models were plotted in axes of abscissas and ordinates, respectively. The numerical values in the parenthesis are the scores for neutral pH and mildly acidic pH models, respectively.