We present a combined experimental and numerical study of the equilibrium cluster formation in globular-protein solutions under no-added salt conditions. We show that a cluster phase emerges as a result of a competition between a long-range screened Coulomb repulsion and a short-range attraction. A simple effective potential, in which electrostatic repulsion is fixed by experimental conditions and attraction is modeled with a generalized Lennard-Jones potential, accounts in a remarkable way for the wavevector dependence of the X-ray scattering structure factor.

Modeling equilibrium clusters in lysozyme solutions

Sciortino F;Zaccarelli E
2007

Abstract

We present a combined experimental and numerical study of the equilibrium cluster formation in globular-protein solutions under no-added salt conditions. We show that a cluster phase emerges as a result of a competition between a long-range screened Coulomb repulsion and a short-range attraction. A simple effective potential, in which electrostatic repulsion is fixed by experimental conditions and attraction is modeled with a generalized Lennard-Jones potential, accounts in a remarkable way for the wavevector dependence of the X-ray scattering structure factor.
2007
Istituto dei Sistemi Complessi - ISC
INFM
LIQUID PHASE-SEPARATION
PROTEIN SOLUTIONS
TRANSITIONS
SCATTERING
PARTICLES
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/159611
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