Figure 2.

Salt-specific structures studied by MD simulations for T = 300 K. (A) Normalized density distribution g(r) of water (O) and cations (all from chloride salts) around the amide oxygen of the EK-peptide. Inset: g(r) for water and cations around the ALA methyl group. (B) Normalized density distribution g(r) of water (O) and anions around the amide nitrogen of the EK-peptide. Inset left: g(r) for water and anions around the ALA methyl group. (C) Ion coordination in a 0.5 nm shell around the backbone plotted versus average helicity h. Coordination increases upon unfolding due to direct binding to the backbone. (D) Nonpolar and polar ASA of the EK and (AK)₆ peptides plotted versus helicity h. Both nonpolar and polar ASA linearly increase upon unfolding.