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Titolo:
Long-term molecular dynamics simulation of copper azurin: structure, dynamics and functionality
Autore:
Arcangeli, C; Bizzarri, AR; Cannistraro, S;
Indirizzi:
Univ Perugia, Dipartimento Fis, Unita INFM, I-06100 Perugia, Italy Univ Perugia Perugia Italy I-06100 s, Unita INFM, I-06100 Perugia, Italy Univ Tuscia, Dipartimento Sci Ambientali, I-01100 Viterbo, Italy Univ Tuscia Viterbo Italy I-01100 Sci Ambientali, I-01100 Viterbo, Italy
Titolo Testata:
BIOPHYSICAL CHEMISTRY
fascicolo: 3, volume: 78, anno: 1999,
pagine: 247 - 257
SICI:
0301-4622(19990419)78:3<247:LMDSOC>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTRAMOLECULAR ELECTRON-TRANSFER; SITE MUTATED AZURINS; PSEUDOMONAS-AERUGINOSA; PLASTOCYANIN; PROTEIN; WATER; HYDRATION; TIME;
Keywords:
azurin; electron transfer; molecular dynamics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Cannistraro, S Univ Perugia, Dipartimento Fis, Unita INFM, I-06100 Perugia, Italy Univ Perugia Perugia Italy I-06100 I-06100 Perugia, Italy
Citazione:
C. Arcangeli et al., "Long-term molecular dynamics simulation of copper azurin: structure, dynamics and functionality", BIOPHYS CH, 78(3), 1999, pp. 247-257

Abstract

A long-term molecular dynamics simulation (1.1 ns), at 300 K, of fully hydrated azurin has been performed to put into relationship the protein dynamics to functional properties with particular attention to those structural elements involved in the electron transfer process. A detailed analysis of the root mean square deviations and fluctuations and of the intraprotein H-bonding pattern has allowed us to demonstrate that a rigid arrangement of the beta-stranded protein skeleton is maintained during the simulation run, while a large mobility is registered in the solvent-exposed connecting regions (turns) and in the alpha-helix. Moreover, the structural elements, likely involved in the electron transfer path, show a stable H-bonding arrangement and low fluctuations. Analysis of the dynamical cross-correlation map has revealed the existence of correlated motions among residues connected by hydrogen bonds and of correlated and anti-correlated motions between regions which are supposed to be involved in the functional process, namely the hydrophobic patch and the regions close to the copper reaction center. The results are briefly discussed also in connection to the current through-bondtunneling model for the electron transfer process. Finally, a comparison with the structural and the dynamical behaviour of plastocyanin, whose structure and functional role are very similar to those of azurin, has been performed. (C) 1999 Elsevier Science B.V. All rights reserved.

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Documento generato il 28/11/20 alle ore 00:43:56