Figure 1

Representation of the C-domain of the CCH protein and related synthetic peptides. (A). Amino acid sequence (one letter code) of the C-domain (residues 69–121) of CCH. The sequence shows relative alternating periodicity of nonpolar (●) and polar (○) amino acids. The stretch of 'h' indicates the putative α-helix predicted by secondary-structure algorithms. The bars denote the location of the two 16-residue repeats of binary structural periodicity of polar/non polar amino acids. (B). Such a motif was used to design the synthetic peptide-1. The amino acid sequence of peptide-1 is arranged into an α-helix (C) and into a β-sheet conformation (D). Positively and negatively charged amino acids are in blue and red, respectively and hydrophobic amino acids are bold cycled.