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