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Titolo:
Recurrence analysis of hydration effects on nonlinear protein dynamics: multiplicative scaling and additive processes
Autore:
Manetti, C; Giuliani, A; Ceruso, MA; Webber, CL; Zbilut, JP;
Indirizzi:
Rush Univ, Dept Mol Biophys & Physiol, Chicago, IL 60612 USA Rush Univ Chicago IL USA 60612 l Biophys & Physiol, Chicago, IL 60612 USA Univ Rome La Sapienza, Dept Chem, I-00185 Rome, Italy Univ Rome La Sapienza Rome Italy I-00185 Dept Chem, I-00185 Rome, Italy Ist Super Sanita, TCE Lab, I-00161 Rome, Italy Ist Super Sanita Rome Italy I-00161 Sanita, TCE Lab, I-00161 Rome, Italy CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, New York, NY 10029 USA CUNYMt Sinai Sch Med New York NY USA 10029 ophys, New York, NY 10029 USA Loyola Univ, Med Ctr, Dept Physiol, Maywood, IL 60153 USA Loyola Univ Maywood IL USA 60153 Ctr, Dept Physiol, Maywood, IL 60153 USA Rush Univ, Dept Mol Biophys & Physiol, Chicago, IL 60612 USA Rush Univ Chicago IL USA 60612 l Biophys & Physiol, Chicago, IL 60612 USA
Titolo Testata:
PHYSICS LETTERS A
fascicolo: 5-6, volume: 281, anno: 2001,
pagine: 317 - 323
SICI:
0375-9601(20010402)281:5-6<317:RAOHEO>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-DYNAMICS; CLUSTER-ANALYSIS; QUANTIFICATION ANALYSIS; ENERGY LANDSCAPE; BINDING DOMAIN; SIMULATION; SPECTROSCOPY; FLUCTUATIONS; TEMPERATURE; DEPENDENCE;
Keywords:
recurrence quantification; molecular dynamics; hydration; noise;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Zbilut, JP Rush Univ, Dept Mol Biophys & Physiol, 1653 W Congress, Chicago, IL 60612 USA Rush Univ 1653 W Congress Chicago IL USA 60612 go, IL 60612 USA
Citazione:
C. Manetti et al., "Recurrence analysis of hydration effects on nonlinear protein dynamics: multiplicative scaling and additive processes", PHYS LETT A, 281(5-6), 2001, pp. 317-323

Abstract

The potential energy time series obtained from molecular dynamics simulations of the B1 domain of protein G and plastocyanin both in vacuo and in water were analyzed by means of recurrence quantification analysis. This methodology is robust for nonlinear, nonstationary processes, and demonstrated the existence of a flat recurrence spectrum occurring beyond a previously described scaling region of protein dynamics, as well as the existence of clustered modes of very long period (approximately 500 ps) elicited by the solvent. The number of these modes was approximately related to the number of structural domains of the studied proteins. Thus the methodology may be useful to distinguish processes intrinsic to protein folding dynamics from those which develop from hydration. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/20 alle ore 14:45:12