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Titolo:
A molecular dynamics simulation study of the solvent isotope effect on copper plastocyanin
Autore:
Guzzi, R; Arcangeli, C; Bizzarri, AR;
Indirizzi:
Univ Calabria, Dipartmento Fis, Unita INFM, I-87030 Rende, Italy Univ Calabria Rende Italy I-87030 Fis, Unita INFM, I-87030 Rende, Italy Univ Tuscia, Dipartimento Sci Ambientali, Unita INFM, I-01100 Viterbo, Italy Univ Tuscia Viterbo Italy I-01100 li, Unita INFM, I-01100 Viterbo, Italy
Titolo Testata:
BIOPHYSICAL CHEMISTRY
fascicolo: 1, volume: 82, anno: 1999,
pagine: 9 - 22
SICI:
0301-4622(19991115)82:1<9:AMDSSO>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN DYNAMICS; POPLAR PLASTOCYANIN; MD SIMULATION; WATER; HYDRATION; DIFFUSION; MYOGLOBIN; RESOLUTION; INTERFACE; CRYSTALS;
Keywords:
plastocyanin; solvent isotope; molecular dynamics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Guzzi, R Univ Calabria, Dipartmento Fis, Unita INFM, I-87030 Rende, Italy Univ Calabria Rende Italy I-87030 ta INFM, I-87030 Rende, Italy
Citazione:
R. Guzzi et al., "A molecular dynamics simulation study of the solvent isotope effect on copper plastocyanin", BIOPHYS CH, 82(1), 1999, pp. 9-22

Abstract

The effect of heavy water on the structure and dynamics of copper plastocyanin as well as on some aspects of the solvent dynamics at the protein-solvent interfacial region have been investigated by molecular dynamics simulation. The simulated system has been analyzed in terms of the atomic root mean square deviation and fluctuations, intraprotein H-bond pattern, dynamicalcross-correlation map and the results have been compared with those previously obtained for plastocyanin in H2O (Ciocchetti et al. Biophys. Chem. 69 (1997), 185-198). The simulated plastocyanin structure in the two solvents,averaging 1 ns, is very similar along the beta-structure regions, while the most significant differences are registered, analogous to the turns and the regions likely involved in the electron transfer pathway. Moreover, plastocyanin in D2O shows an increase in the number of both the intraprotein H-bonds and the residues involved in correlated motions. An analysis of the protein-solvent coupling evidenced that D2O makes the H-bond formation more difficult with the solvent molecules for positively charged and polar residues, while an opposite trend is observed for negatively charged residues. On the other hand, the frequency of exchange of the solvent molecules involved in the protein-solvent H-bond formation is significantly depressed in D2O. The results are discussed also in connection with protein functionality and briefly with some experimental results connected with the thermostability of proteins in D2O, (C) 1999 Elsevier Science B.V. All rights reserved.

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Documento generato il 28/11/20 alle ore 00:47:21