Fig. 8From: Mapping side chain interactions at protein helix terminiGeneral hydrophobic pair motifs at the N-terminus. Motifs detected after a general hydrophobic residue identifier (‘h’) is substituted for the hydrophobic residues {Phe, Leu, Val, Met, Ile}, shown with example structures and global and peak-cluster (*) motif data (Abundance/Overrepresentation/Pvalue). Exemplar width is proportional to motif abundance in the corresponding cluster/geometry, while exemplar colour is proportional to overrepresentation. For N’h-N4h, all exemplars are shown, including those that correspond to clusters in which the motif is underrepresented, in order to emphasize that the motif is generally underrepresented in the capping box geometries. The map for N”h-N4h reveals the backbone turn at N’ that positions the N” SC for hydrophobic interaction with the N4 SCBack to article page