As a further measure, the dihedral angles of the peptide residues collected along the trajectory are plotted together in a Ramachandran plot (Fig. ). While most of the accessible space is visited during the REST trajectory, the vast majority of the angles localize in the area around Φ = -75 • and Ψ = +145 • . This region corresponds to the conformation of the PPII helix, a reference structure for disordered conformations. The secondary structure propensity of the peptide conformers was also analyzed via STRIDE and averaged along the trajectory (Fig. , inlet). All amino acids reveal a preferentially disordered conformation ('coil'). Some amino acids, particularly in the center of the sequence, have a propensity < 30 % for a 'turn' motif.