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Helix Predictions

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.


gjb@bioch.ox.ac.uk