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Literature DB >> 15601122

Dielectric modulation of biological water.

Florin Despa¹, Ariel Fernández, R Stephen Berry.

Abstract

We show that water constrained by vicinal hydrophobes undergoes a librational dynamics that lowers the dielectric susceptibility and induces a "redshift" of the relaxation frequency in the hydration shell. The results shed light on the way proteins enhance their intramolecular interactions as they fold or associate.

Entities: Chemical

Mesh：

Substances：
Proteins
Water

Year: 2004 PMID： 15601122 DOI： 10.1103/PhysRevLett.93.228104

Source DB: PubMed Journal: Phys Rev Lett ISSN： 0031-9007 Impact factor: 9.161

Keyword Cloud
Cited

25 in total

1. The origin of long-range attraction between hydrophobes in water.

Authors: Florin Despa; R Stephen Berry
Journal: Biophys J Date: 2006-09-22 Impact factor: 4.033

2. An extended dynamical hydration shell around proteins.

Authors: Simon Ebbinghaus; Seung Joong Kim; Matthias Heyden; Xin Yu; Udo Heugen; Martin Gruebele; David M Leitner; Martina Havenith
Journal: Proc Natl Acad Sci U S A Date: 2007-12-19 Impact factor: 11.205

3. Antifreeze proteins at the ice/water interface: three calculated discriminating properties for orientation of type I proteins.

Authors: Andrzej Wierzbicki; Pranav Dalal; Thomas E Cheatham; Jared E Knickelbein; A D J Haymet; Jeffry D Madura
Journal: Biophys J Date: 2007-05-25 Impact factor: 4.033

10. Solvent Stokes' shifts revisited: application and comparison of Thompson-Schweizer-Chandler-Song-Marcus theories with Ooshika-Bakshiev-Lippert theories.

Authors: William Kirk
Journal: J Phys Chem A Date: 2008-12-25 Impact factor: 2.781

Dielectric modulation of biological water.

1. The origin of long-range attraction between hydrophobes in water.

2. An extended dynamical hydration shell around proteins.

3. Antifreeze proteins at the ice/water interface: three calculated discriminating properties for orientation of type I proteins.

4. Conformational sampling of peptides in cellular environments.

5. Explanation of the stability of thermophilic proteins based on unique micromorphology.

6. Minimizing frustration by folding in an aqueous environment.

7. Hydrophobe-water interactions: methane as a model.

8. Hydration profiles of amyloidogenic molecular structures.

9. Amyloid oligomer formation probed by water proton magnetic resonance spectroscopy.

10. Solvent Stokes' shifts revisited: application and comparison of Thompson-Schweizer-Chandler-Song-Marcus theories with Ooshika-Bakshiev-Lippert theories.