Supporting MD trajectories for the paper "In Situ Captured Antibacterial Action of Membrane-Incising Peptide Lamellae"

Molecular dynamics trajectories from the production runs of single beta-peptide strands in water + 150 mM NaCl + 50:1 MePO4^(2-):peptide. Altogether 8 runs were performed, each one starting from a different helical conformation (H10, H12 and H14, both positive and negative winding) of the peptide. In the first half (500 ns) of the simulation, the intra-chain hydrogen bonds responsible for the actual helix were kept together by distance restraints. In the second half (again 500 ns), these restraints were instantaneously lifted and the system was left to evolve from the same state. In all cases the helical structure unwound in a very short time (under 100 ns), and did not refold in any helix.