Phase separation and dynamical arrest for particles interacting with mixed potentials--the case of globular proteins revisited
Abstract
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
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@article{arxiv.1101.4447,
title = {Phase separation and dynamical arrest for particles interacting with mixed potentials--the case of globular proteins revisited},
author = {Thomas Gibaud and Frederic Cardinaux and Johan Bergenholtz and Anna Stradner and Peter Schurtenberger},
journal= {arXiv preprint arXiv:1101.4447},
year = {2012}
}