Recent discoveries have shown that intrinsically disordered proteins (IDPs), which lack of a folded structure, can undergo liquid-liquid phase separation to form dynamic assemblies. These assemblies behave like liquid droplets and are closely related to membraneless organelles and pathological aggregates. Much work has been directed toward understanding the molecular mechanism of the phase behavior and how one can predict the phase boundaries from the composing IDP sequences. Due to the scale of these systems, atomistic simulations would be severely limited and even coarse-grained models cannot be used for scanning the relevant sequence space. Here we show that many of these sequences follow the properties of homopolymers. We are therefore able to predict the phase behavior of IDP sequences using only single-molecular properties and highly-efficient single-chain simulations.

Models for liquid-liquid phase separation of disordered proteins

2019 Spring National Meeting

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.