In addition, we considered three polypeptides consisting of 15 or 16 alanine residues, with structures that were extracted from a molecular dynamics simulation (see Section S1.1 in the Supporting Information for details). These represent polyalanine-15 in an α-helical and in a β-strand conformation, as well as a polyalanine-16 in the conformation of a β-hairpin (the additional alanine residue is used to connect the two antiparallel β-strands). However, as all three structures of polyalanine-15/16 are not stable during the molecular dynamics simulation, they start to deviate substantially from idealized structures (see Fig. ), and some of their dihedral angles do not fit into their respective regions on the Ramachandran plot anymore (see Figs. S10-S12 in the Supporting Information). While the α-helix and the β-hairpin are still recognizable, the β-strand structure starts to approach a random coil. Results for additional snapshots along the molecular dynamics trajectory are shown in Figs. S15-S17 in the Supporting Information.