Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
WATER DYNAMICAL ANOMALIES EVIDENCED BY MOLECULAR-DYNAMICS SIMULATIONSAT THE SOLVENT-PROTEIN INTERFACE
Autore:
ROCCHI C; BIZZARRI AR; CANNISTRARO S;
Indirizzi:
UNIV PERUGIA,DIPARTIMENTO FIS,UNITA INFM I-06100 PERUGIA ITALY UNIV PERUGIA,DIPARTIMENTO FIS,UNITA INFM I-06100 PERUGIA ITALY UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI I-01100 VITERBO ITALY
Titolo Testata:
Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics
fascicolo: 3, volume: 57, anno: 1998,
parte:, B
pagine: 3315 - 3325
SICI:
1063-651X(1998)57:3<3315:WDAEBM>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
COPPER PLASTOCYANIN; DISORDERED MEDIA; RESIDENCE TIME; HYDRATION; DIFFUSION; MYOGLOBIN; STATES; MODEL; TRANSITIONS; RELAXATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
68
Recensione:
Indirizzi per estratti:
Citazione:
C. Rocchi et al., "WATER DYNAMICAL ANOMALIES EVIDENCED BY MOLECULAR-DYNAMICS SIMULATIONSAT THE SOLVENT-PROTEIN INTERFACE", Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics, 57(3), 1998, pp. 3315-3325

Abstract

We present a computer simulation picture of the dynamical behavior, at room temperature, of water in the region close to a protein surface. We analyzed the probability distribution of water molecules diffusingnear the surface, and we found that it deviates from a Gaussian, which is predicted for Brownian particles. Consistently, the mean square displacements of water oxygens show a sublinear trend with time. Moreover, the relaxation of hydration layers around the whole protein is found to follow a stretched exponential decay, typical of complex systems, which could as well be ascribed to the non-Gaussian shape of the propagator. In agreement with such findings, the analysis of water translational and reorientational diffusion showed that not only are the solvent molecule motions hindered in the region close to the protein surface, but also the very nature of the particle diffusive processes, both translational and rotational, is affected. The deviations from the bulk water properties, which put into evidence a deep influence exertedby the protein on the solvent molecule motion, are discussed in connection with the presence of spatial (protein surface roughness) and temporal (distribution of water residence times) disorder inherent in thesystem.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 23:43:53