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Titolo:
The interface between a protein crystal and an aqueous solution and its effects on nucleation and crystal growth
Autore:
Haas, C; Drenth, J;
Indirizzi:
Univ Groningen, Biophys Chem Lab, NL-9747 AG Groningen, Netherlands Univ Groningen Groningen Netherlands NL-9747 AG G Groningen, Netherlands
Titolo Testata:
JOURNAL OF PHYSICAL CHEMISTRY B
fascicolo: 2, volume: 104, anno: 2000,
pagine: 368 - 377
SICI:
1520-6106(20000120)104:2<368:TIBAPC>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIQUID-PHASE-SEPARATION; ANGLE NEUTRON-SCATTERING; LYSOZYME SOLUTIONS; LIGHT-SCATTERING; DIFFUSIVE EVOLUTION; METASTABLE PHASES; CRITICAL-POINT; WATER SOLUTION; SIMPLE FLUIDS; AGGREGATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
70
Recensione:
Indirizzi per estratti:
Indirizzo: Drenth, J Univ Groningen, Biophys Chem Lab, Nijenborgh 4, NL-9747 AG Groningen, Netherlands Univ Groningen Nijenborgh 4 Groningen Netherlands NL-9747 AG ds
Citazione:
C. Haas e J. Drenth, "The interface between a protein crystal and an aqueous solution and its effects on nucleation and crystal growth", J PHYS CH B, 104(2), 2000, pp. 368-377

Abstract

In this paper we report calculations of the concentration profile and the Gibbs free energy of the interface between a protein crystal and an aqueoussolution, The calculations are based on a simple, realistic expression forthe Gibbs free energy of the solution, which reproduces characteristic features of the protein-water phase diagram, such as the presence of a metastable liquid-liquid immiscibility region, An equation is derived which expresses the coefficient for the contribution of concentration gradients to the Gibbs free energy of the solution in terms of the interaction potential between the protein molecules, Calculations are presented which show that the presence of a metastable liquid-liquid immiscibility region in the phase diagram has a profound effect on the properties of the interface between a crystal and the solution, Near and below the critical temperature for metastable liquid-liquid phase separation the protein crystal is covered by a thinliquid film with a high protein concentration. This surface film causes a substantial lowering of the surface energy of the crystal. The effects of this film on the kinetic processes associated with the nucleation and the further growth of protein crystals are discussed.

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Documento generato il 28/09/20 alle ore 15:37:09