Figure 1 - full size

 

Figure 1.
Fig. 1. (a) Cartoon of the three-dimensional structure of the intact bPrP(23-230). Helices are green, -strands are cyan, segments with nonregular secondary structure within the C-terminal domain are yellow, and the flexibly disordered "tail" of residues 23-121 is represented by 108 yellow dots, each of which represents a residue of the tail (the numeration for hPrP is used, and the insertions and deletions are placed according to the alignment in ref. 23). (b) Stereo-view of an all-heavy atom presentation of the globular domain in bPrP(23-230), with residues 121-230, in the same orientation as in a. The backbone is shown as a green spline function through the C^ positions, hydrophobic side chains are yellow, and polar and charged side chains are violet. (c and d) Surface views of the globular domains of bPrP and hPrP, respectively. The orientation of the molecule is slightly changed relative to a, so that the residue 186 is approximately in the center. The electrostatic surface potential is indicated in red (negative charge), white (neutral), and blue (positive charge). The figures were prepared with the program MOLMOL (42).