  The influence of the salts KCl, NaCl, and NaI at molar concentrations on the
{\alpha}-helical folding kinetics of the alanine-based oligopeptide
Ace-AEAAAKEAAAKA-Nme is investigated by means of (explicit-water) molecular
dynamics simulations and a diffusional analysis. The mean first passage times
for folding and unfolding are found to be highly salt-specific. In particular,
the folding times increase about one order of magnitude for the sodium salts.
The drastic slowing down can be traced back to long-lived, compact
configurations of the partially folded peptide, in which sodium ions are
tightly bound by several carbonyl and carboxylate groups. This multiple
trapping is found to lead to a non-exponential residence time distribution of
the cations in the first solvation shell of the peptide. The analysis of
{\alpha}-helical folding in the framework of diffusion in a reduced
(one-dimensional) free energy landscape further shows that the salt not only
specifically modifies equilibrium properties, but also induces kinetic barriers
due to individual ion binding. In the sodium salts, for instance, the peptide's
configurational mobility (or "diffusivity") can decrease about one order of
magnitude. This study demonstrates the highly specific action of ions and
highlights the intimate coupling of intramolecular friction and solvent effects
in protein folding.
