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 (Vb ≅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.
|Journal||Physical Review Letters|
|State||Published - Nov 29 2004|
Bibliographical noteFunding Information:
We acknowledge the support of a grant from the National Science Foundation.
ASJC Scopus subject areas
- Physics and Astronomy (all)