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Titolo:
Molecular dynamics simulation and essential dynamics study of mutated plastocyanin: structural, dynamical and functional effects of a disulfide bridge insertion at the protein surface
Autore:
Arcangeli, C; Bizzarri, AR; Cannistraro, S;
Indirizzi:
Univ Tuscia, INFM, 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: 92, anno: 2001,
pagine: 183 - 199
SICI:
0301-4622(20010918)92:3<183:MDSAED>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
SCANNING-TUNNELING-MICROSCOPY; ELECTRON-TRANSFER; POPLAR PLASTOCYANIN; COPPER PROTEIN; CYTOCHROME-C; RESOLUTION; AZURIN; WATER; TIME; COMPLEXES;
Keywords:
disulphide bond; poplar plastocyanin; molecular dynamics; essential dynamics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Cannistraro, S Univ Tuscia, INFM, Dipartimento Sci Ambientali, Via S Camillo Lellis,Blocco D, I-01100 Viterbo, Italy Univ Tuscia Via S Camillo Lellis,Blocco D Viterbo Italy I-01100
Citazione:
C. Arcangeli et al., "Molecular dynamics simulation and essential dynamics study of mutated plastocyanin: structural, dynamical and functional effects of a disulfide bridge insertion at the protein surface", BIOPHYS CH, 92(3), 2001, pp. 183-199

Abstract

A molecular dynamics simulation (1.1 ns) at 300 K, of fully hydrated Ile21Cys, Glu25Cys plastocyanin mutant has been performed to investigate the structural, dynamical and functional effects of a disulfide bridge insertion at the surface of the protein. A detailed analysis of the root mean square fluctuations, H-bonding pattern and dynamical cross-correlation map has beenperformed. An essential dynamics method has also been applied as complementary analysis to identify concerted motions (essential modes), that could be relevant to the electron transfer function. The results have been compared with those previously obtained for wild-type plastocyanin and have revealed that the mutant shows a different pattern of H-bonds, with several interactions lost and a higher flexibility, especially around the electron transfer copper site. The analysis of dynamical cross-correlation map and of essential modes, has shown that the mutant performs different functional concerted motions, which might be related to the binding recognition with its electron transfer partners in comparison with the wild-type protein. (C) 2001Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 01:00:25