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We examine the applicability of the extended law of corresponding states(ELCS) to equilibrium and non equilibrium features of the state diagram of theglobular protein lysozyme. We provide compelling evidence that the ELCScorrectly reproduces the location of the binodal for different ionic strengths,but fails in describing the location of the arrest line. We subsequently useMode Coupling Theory (MCT) to gain additional insight into the origin of theseobservations. We demonstrate that while the critical point and the connectedbinodal and spinodal are governed by the integral features of the interactionpotential described by the normalized second virial coefficient, the arrestline is mainly determined by the attractive well depth or bond strength. Thisarticle is published in Soft Matter. The reference is: DOI: 10.1039/c0sm01175d

Phase separation and dynamical arrest for particles interacting with mixed potentials--the case of globular proteins revisited