Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
MOLECULAR-DYNAMICS OF COPPER PLASTOCYANIN - SIMULATIONS OF STRUCTURE AND DYNAMICS AS A FUNCTION OF HYDRATION
Autore:
WANG CX; BIZZARRI AR; XU YW; CANNISTRARO S;
Indirizzi:
UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI,SEZIONE CHIM & FIS I-01100 VITERBO ITALY UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI,SEZIONE CHIM & FIS I-01100 VITERBO ITALY UNIV SCI & TECHNOL CHINA,CTR FUNDAMENTAL PHYS HEFEI 230036 PEOPLES R CHINA UNIV PERUGIA,CNR,UNITA INFM,DIPARTIMENTO FIS I-06100 PERUGIA ITALY
Titolo Testata:
Chemical physics
fascicolo: 1, volume: 183, anno: 1994,
pagine: 155 - 166
SICI:
0301-0104(1994)183:1<155:MOCP-S>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
COMPUTER-SIMULATION; FORCE-FIELD; TEMPERATURE-DEPENDENCE; POTENTIAL FUNCTIONS; NEUTRON-SCATTERING; WATER; MYOGLOBIN; PROTEIN; METALLOPROTEINS; PARVALBUMIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
C.X. Wang et al., "MOLECULAR-DYNAMICS OF COPPER PLASTOCYANIN - SIMULATIONS OF STRUCTURE AND DYNAMICS AS A FUNCTION OF HYDRATION", Chemical physics, 183(1), 1994, pp. 155-166

Abstract

Molecular dynamics simulations of copper plastocyanin were carried out to study protein structure and dynamics as a function of hydration. The simulations of plastocyanin were performed at 300 K in the presence of 44, 80, 228, 682, 2516 water molecules, respectively. For each different hydrated system, the simulation covered 110 ps; the trajectories of the last 80 ps were used for analysis. Structural and dynamical properties of the protein are considerably altered upon addition of water. The gyration ratio value indicates that the most compact structure is obtained in the presence of 80 water molecules. Both the RMS deviations from the initial structure and the fluctuations of the protein atoms depend significantly on the number of hydration water molecules. The largest RMS deviations are obtained at intermediate hydration level, while the smallest value is recorded at full hydration. The RMS fluctuations are minimized in the presence of 80 water molecules and maximized at high hydration level. The interplay among protein dynamics, hydration water and the aminoacid residue properties is discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 00:25:30