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Titolo:
Relaxational dynamics of water molecules at protein surface
Autore:
Dellerue, S; Bellissent-Funel, MC;
Indirizzi:
CEA Saclay, CNRS, Leon Brillouin Lab, CEA, F-91191 Gif Sur Yvette, France CEA Saclay Gif Sur Yvette France F-91191 F-91191 Gif Sur Yvette, France
Titolo Testata:
CHEMICAL PHYSICS
fascicolo: 2-3, volume: 258, anno: 2000,
pagine: 315 - 325
SICI:
0301-0104(20000815)258:2-3<315:RDOWMA>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
INELASTIC NEUTRON-SCATTERING; SINGLE-PARTICLE DYNAMICS; LOW-FREQUENCY DYNAMICS; SUPERCOOLED WATER; SUPEROXIDE-DISMUTASE; GLASS-TRANSITION; GLOBULAR PROTEIN; HYDRATION WATER; MYOGLOBIN; DIFFUSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Bellissent-Funel, MC CEA Saclay, CNRS, Leon Brillouin Lab, CEA, F-91191 Gif Sur Yvette, France CEA Saclay Gif Sur Yvette France F-91191 te, France
Citazione:
S. Dellerue e M.C. Bellissent-Funel, "Relaxational dynamics of water molecules at protein surface", CHEM PHYS, 258(2-3), 2000, pp. 315-325

Abstract

Relaxational dynamics of water molecules at the surface of a C-phycocyaninprotein is studied by high resolution quasi-elastic neutron scattering. The neutron quasi-elastic spectra are well described by the alpha-relaxation process of mode coupling theory of supercooled liquids. The relaxation times of interfacial water exhibit a power law dependence on the wave vector Q. The average diffusion coefficient is 10 times lower than that of bulk water. This confirms that there is a retardation of water molecules at the protein surface which is in good agreement with the results of water at the surface of hydrophilic model systems. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 10:00:33