Nucleation in a simple model for protein solutions with anisotropic interactions.
A lattice analog of density functional theory is used to explore the structural and thermodynamic properties of critical nuclei in mixtures of particles with attractive anisotropic interactions. Protein molecules are assumed to occupy the sites on a regular cubic lattice, with effective directional interactions that mimic hydrogen bonding and the solvation forces induced by water. Interaction parameters are chosen to qualitatively reproduce the phase behavior of protein solutions. Our model predicts that critical nuclei of the solidlike phase have nonspherical shapes, and that their specific geometry depends on the nature of the anisotropic interactions. Molecules tend to align in distinctive ways in the core and in the interfacial region of these critical clusters, and the width and structure of the interface are highly affected by the presence of a metastable fluid-fluid critical point. Close to the critical region, the height of the barrier to nucleation is strongly reduced; this effect is enhanced by increasing the anisotropy of the intermolecular interactions. Unlike systems with short-range isotropic interactions, nucleation in our model is initiated by highly ordered clusters in which the order-disorder transition is confined to the interfacial region.
Talanquer
V
V
Department of Chemistry, University of Arizona, Tucson, AZ 85721, USA.
D016880:Anisotropy; D001665:Binding Sites; D003198:Computer Simulation; D003460:Crystallization / Q000379:methods*; D019281:Dimerization; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012996:Solutions
D046912:Multiprotein Complexes; D011506:Proteins; D012996:Solutions