Phase separation and dynamical arrest for particles interacting with mixed potentials--the case of globular proteins revisited
arXiv:1101.4447 · doi:10.1039/c0sm01175d
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
References in corpus (1)
Cited by in corpus (11)
- Intermittent dynamics and logarithmic domain growth during the spinodal decomposition of a glass-forming liquid
- Extended law of corresponding states for protein solutions
- Design rules for the self-assembly of a protein crystal
- How soft repulsion enhances the depletion mechanism
- Unexpected decoupling of stretching and bending modes in protein gels
- Transient stress evolution in repulsion and attraction dominated glasses
- Universal effective interactions of globular proteins close to liquid-liquid phase separation: corresponding-states behavior reflected in the structure factor
- Filamentous phages as building blocks for reconfigurable and hierarchical self-assembly
- Phase separation and dynamical arrest of protein solutions dominated by short-range attractions
- Protein solutions close to liquid-liquid phase separation exhibit a universal osmotic equation of state and dynamical behavior
- Phase separation of stable colloidal clusters