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Title: Effects of hydration water on protein methyl group dynamics insolution

Abstract

Elastic and quasielastic neutron scattering experiments have been used to investigate the dynamics of methyl groups in a protein-model hydrophobic peptide in solution. The results suggest that, when the hydrophobic side chains are hydrated by a single hydration water layer, the only allowed motions are confined and attributed to librational and rotational movement associated with the methyl groups. They provide unique experimental evidence that the structural and dynamical properties of the interfacial water strongly influence the side-chain dynamics and the activation of diffusive motion.

Authors:
; ;
Publication Date:
Research Org.:
COLLABORATION - Institut LaueLangevin/France
OSTI Identifier:
910600
Report Number(s):
LBNL-63261
Journal ID: ISSN 1063-651X; PLEEE8; TRN: US0704270
DOE Contract Number:  
DE-AC02-05CH11231
Resource Type:
Journal Article
Resource Relation:
Journal Name: Physical Review E; Journal Volume: 75; Journal Issue: 4pt1; Related Information: Journal Publication Date: 04/2007
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 72 PHYSICS OF ELEMENTARY PARTICLES AND FIELDS; CHAINS; HYDRATION; NEUTRONS; PEPTIDES; PROTEINS; SCATTERING; WATER

Citation Formats

Russo D, Hura GL, and Copley JRD. Effects of hydration water on protein methyl group dynamics insolution. United States: N. p., 2007. Web.
Russo D, Hura GL, & Copley JRD. Effects of hydration water on protein methyl group dynamics insolution. United States.
Russo D, Hura GL, and Copley JRD. Mon . "Effects of hydration water on protein methyl group dynamics insolution". United States. doi:.
@article{osti_910600,
title = {Effects of hydration water on protein methyl group dynamics insolution},
author = {Russo D and Hura GL and Copley JRD},
abstractNote = {Elastic and quasielastic neutron scattering experiments have been used to investigate the dynamics of methyl groups in a protein-model hydrophobic peptide in solution. The results suggest that, when the hydrophobic side chains are hydrated by a single hydration water layer, the only allowed motions are confined and attributed to librational and rotational movement associated with the methyl groups. They provide unique experimental evidence that the structural and dynamical properties of the interfacial water strongly influence the side-chain dynamics and the activation of diffusive motion.},
doi = {},
journal = {Physical Review E},
number = 4pt1,
volume = 75,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}