Dielectric modulation of biological water

A model which shows the librational dynamics undergone by water constrained by vicinal hydrophobes, which lowers the dielectric susceptibility and induces a 'redshift' of the relaxation frequency in the hydration shell was presented. The reduction of H-bond exchange possibilities of water molecules at a hydrophobic interface was analyzed. Water molecules were found to exchange H bonds with neighbours at a fast rate (V_b ≅1.7 × 10 ¹³ s^-1 at room temperature. The results also demonstrated the way in which proteins enhance their intramolecular interactions as they fold or associate.