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. 2005 Jan 12;102(3):646–650. doi: 10.1073/pnas.0409008102

Fig. 4.

Fig. 4.

Polypeptide segment 165–172 in the energy-minimized NMR structures of bPrP, hPrP, mPrP, shPrP, and ePrP and in mPrP[N174T] and mPrP[S170N,N174T]. The backbone is represented by a spline function through the Cα positions. The radius of the cylindrical rods is proportional to the mean backbone displacement per residue, as evaluated after superposition for best fit of the atoms N, Cα, and C′ of the residues 166–172 in the 20 energy-minimized conformers used to represent the NMR structures. For the amino acid sequences, see Fig. 1B.