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Titolo:
HYDROGEN-BOND ANALYSIS BY MD SIMULATION OF COPPER PLASTOCYANIN AT DIFFERENT HYDRATION LEVELS
Autore:
BIZZARRI AR; WANG CX; CHEN WZ; CANNISTRARO S;
Indirizzi:
UNIV PERUGIA,DIPARTIMENTO FIS,CNR,UNITA INFM I-06100 PERUGIA ITALY UNIV PERUGIA,DIPARTIMENTO FIS,CNR,UNITA INFM I-06100 PERUGIA ITALY UNIV SCI & TECHNOL CHINA,CTR FUNDAMENTAL PHYS HEFEI 230036 PEOPLES R CHINA UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI,SEZ CHIM & FIS I-01100 VITERBO ITALY
Titolo Testata:
Chemical physics
fascicolo: 2-3, volume: 201, anno: 1995,
pagine: 463 - 472
SICI:
0301-0104(1995)201:2-3<463:HABMSO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-DYNAMICS; PROTEIN DYNAMICS; WATER; MYOGLOBIN; INTEGRATION; SCATTERING; DEPENDENCE; SYSTEMS; TIME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
A.R. Bizzarri et al., "HYDROGEN-BOND ANALYSIS BY MD SIMULATION OF COPPER PLASTOCYANIN AT DIFFERENT HYDRATION LEVELS", Chemical physics, 201(2-3), 1995, pp. 463-472

Abstract

Hydrogen bond interactions in copper plastocyanin aqueous solutions have been investigated in details by computer simulation, Molecular dynamics simulations of the protein in the presence of a different numberof water molecules (80, 228, 682, 2516) have been performed for 110 picoseconds, Intraprotein hydrogen bonds occurring on the MD simulations are investigated and compared to the hydrogen bonds detected in the crystal structure as obtained from X-ray data. Protein-water hydrogen bonds are analyzed in terms of the average number of hydrogen bonds formed by each aminoacid residue and in terms of the number of differentwater molecules forming hydrogen bonds with each amino-acid residue during the simulation time. A strong influence on the protein-solvent interface of the electrical character of the aminoacid residues involved in the protein-water hydrogen bonds is evidenced, The results point out the crucial role played by the hydration level on the organizationof the hydrogen bond network surrounding a protein molecule and on the protein-solvent coupling. The behaviour of the protein-solvent hydrogen bonds is discussed in connection with the protein dynamics.

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Documento generato il 28/11/20 alle ore 00:36:37