The effect of the range of interaction on the phase diagram of a globular protein

Abstract

Thermodynamic perturbation theory is applied to the model of globular proteins studied by ten Wolde and Frenkel (Science 277, pg. 1976) using computer simulation. It is found that the reported phase diagrams are accurately reproduced. The calculations show how the phase diagram can be tuned as a function of the lengthscale of the potential.

arXiv comment20 pages, 5 figures

References in corpus (4)

• Theory and simulation of short-range models of globular protein solutions
• Crystal nucleation for a model of globular proteins
• Thermodynamic perturbation theory of the phase behaviour of colloid / interacting polymer mixtures
• A Finite-Size Scaling Study of a Model of Globular Proteins

Cited by in corpus (6)

• Theoretical evidence for a dense fluid precursor to crystallization
• A dynamical theory of nucleation for colloids and macromolecules
• Patchy sticky hard spheres: analytical study and Monte Carlo simulations
• The low-density/high-density liquid phase transition for model globular proteins
• Nonclassical Nucleation Pathways in Liquid Condensation Revealed by Simulation and Theory
• The seeding method: A test case for classical nucleation theory in small systems