The conformation of proteins in solution is influenced by the presence of ions, but the driving force behind this phenomenon is not well-understood.  We believe that ions modulate peptide hydration, causing it to experience a shift in its conformational equilibrium.  Molecular dynamics simulations have been performed on a peptide with the primary structure AEAAAEA in different saline environments to test this hypothesis.  Ion effects on the electrostatic repulsion between side chains, ion-side chain binding, as well as peptide hydration have been studied, since these have been referenced as potential driving forces for this phenomenon.  Salts included in this study were NaCl and KCl at concentrations of 0.5, 1.0 and 2.0 M.  Simulation trajectories were analyzed with radial distribution functions, the calculation of preferential interaction parameters, calculated circular dichroism spectra, and various free energy calculations.

Salt effects on the conformational stability of small peptides

243rd National Meeting (2012)

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