Figure 2

Comparison of the amphipathic α-helical domains of α-synuclein and related proteins. Sequences of interest were imported into Swiss-PdbViewer [40], assigned an ideal α-helical structure, and exported as .pdb files. Models were then formatted and exported with RASMol [41], and animations (available with the complete version of this article, online) were compiled with QuickTime Pro. (a) Human α-synuclein residues 1-50, modeled as an α-helix. The initial frame shown here shows just the hydrophilic face of the helix, with acidic residues confined to the center (red) and basic residues at each interface (yellow); the opposite hydrophobic face (shown in the animation online) contains only uncharged residues (white). (b) Human apolipoprotein AI residues 190-231; (c) Arabidopsis thaliana LEA76 residues 1-50; (d) C. elegans LEA residues 351-400; all are modeled as in (a).