Abstract
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.
Original language | English |
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Article number | 228104 |
Journal | Physical Review Letters |
Volume | 93 |
Issue number | 22 |
DOIs | |
State | Published - Nov 29 2004 |
Bibliographical note
Funding Information:We acknowledge the support of a grant from the National Science Foundation.
Funding
We acknowledge the support of a grant from the National Science Foundation.
Funders | Funder number |
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National Science Foundation (NSF) |
ASJC Scopus subject areas
- General Physics and Astronomy