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Fluid-crystal coexistence for proteins and inorganic nanocolloids: Dependence on ionic strength
Author(s) -
Peter Prinsen,
Theo Odijk
Publication year - 2006
Publication title -
the journal of chemical physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.071
H-Index - 357
eISSN - 1089-7690
pISSN - 0021-9606
DOI - 10.1063/1.2336423
Subject(s) - ionic strength , colloid , particle (ecology) , chemistry , donnan potential , phase (matter) , crystal (programming language) , globular protein , virial theorem , thermodynamics , charge (physics) , salt (chemistry) , lysozyme , nanoparticle , chemical physics , materials science , physics , electrolyte , nanotechnology , aqueous solution , crystallography , quantum mechanics , biochemistry , oceanography , organic chemistry , electrode , computer science , geology , galaxy , programming language
We investigate theoretically the fluid-crystal coexistence of solutions of globular charged nanoparticles such as proteins and inorganic colloids. The thermodynamic properties of the fluid phase are computed via the optimized Baxter model P. Prinsen and T. Odijk [J. Chem. Phys. 121, 6525 (2004)]. This is done specifically for lysozyme and silicotungstates for which the bare adhesion parameters are evaluated via the experimental second virial coefficients. The electrostatic free energy of the crystal is approximated by supposing the cavities in the interstitial phase between the particles are spherical in form. In the salt-free case a Poisson-Boltzmann equation is solved to calculate the effective charge on a particle and a Donnan approximation is used to derive the chemical potential and osmotic pressure in the presence of salt. The coexistence data of lysozyme and silicotungstates are analyzed within this scheme, especially with regard to the ionic-strength dependence of the chemical potentials. The latter agree within the two phases provided some upward adjustment of the effective charge is allowed for.Applied Science

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