Five regions are assigned to the helical conformation (23-44, 64-73,
196-205, 278-283, 288-296), with a further 3 possible helical regions
where the prediction is ambiguous (see Ambiguous predictions
below). A helix that has one side exposed to solvent and one that
packs against the hydrophobic protein core often has hydrophobic
residues on the buried face. Accordingly, conserved hydrophobic
residues seen at an spacing give strong supporting
evidence for a predicted helix. The predicted helix at 23-44 shows
this type of pattern, with conserved hydrophobics at 24, 27, 28, 31,
34 and 35. The pattern continues with conserved hydrophobics at 41,
42 and 44, but the conserved proline at 39 suggests that the helix may
contain a kink. Similar patterns are seen for the predicted helices at 64-73,
160-180 (where a kink may occur at 175), and 278-283.