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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}
}
  • This review article describes our neutron scattering experiments made in the past four years for the understanding of the single-particle (hydrogen atom) dynamics of a protein and its hydration water and the strong coupling between them. We found that the key to this strong coupling is the existence of a fragile-to-strong dynamic crossover (FSC) phenomenon occurring at around T L = 225±5 K in the hydration water. On lowering of the temperature toward FSC, the structure of hydration water makes a transition from predominantly the high density form (HDL), a more fluid state, to predominantly the low density form (LDL),more » a less fluid state, derived from the existence of a liquid–liquid critical point at an elevated pressure. We show experimentally that this sudden switch in the mobility of hydration water on Lysozyme, B-DNA and RNA triggers the dynamic transition, at a temperature T D = 220 K, for these biopolymers. In the glassy state, below T D , the biopolymers lose their vital conformational flexibility resulting in a substantial diminishing of their biological functions. We also performed molecular dynamics (MD) simulations on a realistic model of hydrated lysozyme powder, which confirms the existence of the FSC and the hydration level dependence of the FSC temperature. Furthermore, we show a striking feature in the short time relaxation ( β -relaxation) of protein dynamics, which is the logarithmic decay spanning 3 decades (from ps to ns). The long time α -relaxation shows instead a diffusive behavior, which supports the liquid-like motions of protein constituents. We then discuss our recent high-resolution X-ray inelastic scattering studies of globular proteins, Lysozyme and Bovine Serum Albumin. We were able to measure the dispersion relations of collective, intra-protein phonon-like excitations in these proteins for the first time. We found that the phonon energies show a marked softening and at the same time their population increases substantially in a certain wave vector range when temperature crosses over the T D . Thus the increase of biological activities above T D has positive correlation with activation of slower and large amplitude collective motions of a protein.« less
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  • Proteins undergo a number of changes when their temperature is dropped from the physiological range to much lower values. One of the most well-known dynamical changes undergone by proteins in a solid state is a so-called protein glass-transition, which is a dynamic transition occurring at about 200-230K leading to a loss of biological activity.1,2 X-ray diffraction, neutron scattering studies, and dielectric spectroscopy, as well as evidence from NMR relaxation measurements, indicate freezing of slow collective modes of motion below the glass transition temperature.3-8 Various arguments have been presented that connect the transition to solvent participation.1,4,8-10 In addition to the solvent-relatedmore » modes that are frozen below the glass-transition temperature, there are anharmonic motions at temperatures below 200K which are likely to be dominated by methyl group dynamics down to about 100K.2,5,7 Recent neutron-scattering and NMR studies emphasize the role of these modes in low temperature dynamics. 2,5,7,11,12 One of the latest works on the subject by Bajaj et al.11 has reported a structural transition associated with dynamic processes in a solvent-free polypeptide. Thus, protein dynamics at low temperatures are complex and more studies are required to discern their pattern.« less
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