We investigate the ionic strength and temperature dependence of metastability with respect to crystallization in lysozyme solution. The supersaturation limit c* shows a simple scaling relation with salt concentration and, together with the equilibrium solubility c(sat), approximately factorizes into two terms, respectively accounting for electrostatic and temperature effects. The supersaturation ratio S = c*/c(sat) monotonically increases with the addition of salt. While the dependence of solution properties on the ionic strength is consistent with a recent model by Sear and Warren, temperature effects highlight the importance of hydrophobic contributions.

Metastability and supersaturation limit for lysozyme crystallization / M. Carpineti, R. Piazza. - In: PHYSICAL CHEMISTRY CHEMICAL PHYSICS. - ISSN 1463-9076. - 6:7(2004), pp. 1506-1511.

Metastability and supersaturation limit for lysozyme crystallization

M. Carpineti
Primo
;
2004

Abstract

We investigate the ionic strength and temperature dependence of metastability with respect to crystallization in lysozyme solution. The supersaturation limit c* shows a simple scaling relation with salt concentration and, together with the equilibrium solubility c(sat), approximately factorizes into two terms, respectively accounting for electrostatic and temperature effects. The supersaturation ratio S = c*/c(sat) monotonically increases with the addition of salt. While the dependence of solution properties on the ionic strength is consistent with a recent model by Sear and Warren, temperature effects highlight the importance of hydrophobic contributions.
PROTEIN CRYSTAL-GROWTH ; EGG-WHITE LYSOZYME ; GLOBULAR-PROTEINS ; PHASE-BEHAVIOR ; HARD-SPHERES ; SOLUBILITY ; NUCLEATION ; PARTICLES ; CHARGE ; MODEL
2004
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/27865
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