Fig. 2

Nearly 50% of secondary structure assignments were random coils, while the rest were attributed to α-helix, 3-10 helix, turn and bend. Generalized Born implicit-water MD simulations (400 ns) at physiological pH 7.4 of cysteinated and C-terminal amidated homing peptides GASNGINAYLC-NH₂ (A, a–b) and SLWERLAYGIC-NH₂ (B, a–b). a Time evolution of peptide secondary structures and root-mean square-deviations (RMSD, Å). b Percentage of secondary structure distribution among residues showing assignments of known secondary structures in nearly 50% of the simulation time (Average in the last column). The first and last residues have neither backbone dihedrals nor assignments, and were calculated as zero in the average for uniformity