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Titolo:
A patch-antipatch representation of specific protein interactions
Autore:
Hloucha, M; Lodge, JFM; Lenhoff, AM; Sandler, SI;
Indirizzi:
Univ Delaware, Dept Chem Engn, Newark, DE 19716 USA Univ Delaware Newark DE USA 19716 e, Dept Chem Engn, Newark, DE 19716 USA
Titolo Testata:
JOURNAL OF CRYSTAL GROWTH
fascicolo: 1-4, volume: 232, anno: 2001,
pagine: 195 - 203
SICI:
0022-0248(200111)232:1-4<195:APROSP>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIQUID-PHASE-SEPARATION; SUPERSATURATED LYSOZYME SOLUTIONS; 2ND VIRIAL-COEFFICIENT; GLOBULAR-PROTEINS; COLLOIDAL PARTICLES; CRITICAL-BEHAVIOR; BINARY MIXTURE; WATER SOLUTION; SALT-WATER; CRYSTALLIZATION;
Keywords:
biocrystallization; computer simulation; proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
--discip_EC--
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Lenhoff, AM Univ Delaware, Dept Chem Engn, Newark, DE 19716 USA Univ Delaware Newark DE USA 19716 Engn, Newark, DE 19716 USA
Citazione:
M. Hloucha et al., "A patch-antipatch representation of specific protein interactions", J CRYST GR, 232(1-4), 2001, pp. 195-203

Abstract

Protein interactions in solution are manifested in macroscopically measurable thermodynamic properties such as the osmotic second virial coefficient. These interactions are typically characterized by a sensitivity to electrostatic parameters such as pH and ionic strength, and by strong short-range attraction with a pronounced orientational dependence. We describe here a model that embodies all these features, yet is sufficiently compact to allowits use in simulations of dynamic and equilibrium properties. The model treats protein molecules as spheres with relatively weak isotropic contributions to intermolecular interactions. In addition, a discrete number of "patch-antipatch" pairs on the surfaces account for highly specific interactionsthat can arise from geometric complementarity of corresponding areas on the actual molecular surface. Implementation of the model is illustrated for interactions in solution of bovine chymotrypsinogen, based on structural information from crystallographic data. The general trends seen in virial coefficient measurements are captured by the model, despite anomalous featuresthat are thought to result from the importance of the specific interactions. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 28/09/20 alle ore 15:03:40