A simple model of directional interactions for proteins.
We study a simple two patch model of globular protein solutions. The model consists of a hard sphere interaction, together with a weak isotropic attraction, decorated with stronger attractive patch-patch interactions. The isotropic and anisotropic attractions are modeled with square well potentials with an interaction range of 1.2sigma, where sigma is the hard sphere diameter. We have calculated its phase diagram and found a metastable fluid-fluid phase separation curve. We have also obtained the different stable crystal structures at various temperatures. The orientationally ordered, body-centered crystal (bcc-o) lattice is the crystal structure that has the lowest energy; it is stable at lower temperatures and moderate pressures. The orientationally ordered face-centered crystal (fcc) lattice has a higher energy and becomes stable with respect to bcc-o at high pressures and lower temperatures. Finally, at high temperatures when the entropy effect becomes important, the orientational order is lost and an orientationally disordered fcc lattice becomes stable.
Department of Physics, Lehigh University, Bethlehem, Pennsylvania 18015, USA. xil204@lehigh.edu
Xiaofei
X
Li
J D
JD
Gunton
A
A
Chakrabarti
D001665:Binding Sites; D003460:Crystallization; D019281:Dimerization; D019277:Entropy; D008958:Models, Molecular; D009010:Monte Carlo Method; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D011506:Proteins / Q000737:chemistry*; D012996:Solutions; D013816:Thermodynamics
D011506:Proteins; D012996:Solutions