(189k) Molecular Simulations of Liquid-like Assemblies of Intrinsically Disordered Proteins

Authors: 
Dignon, G. L., Lehigh University
Mittal, J., Lehigh University
Zheng, W., Arizona State University
Kim, Y. C., Naval Research Laboratory
Proteins, which undergo liquid-liquid phase separation (LLPS) to form dynamic assemblies within biological systems, have been gaining much attention due to their relevance to membraneless organelles and prospects for material design. Much work has been directed toward understanding the molecular mechanisms of phase behavior and predicting the phase boundaries and dynamics of biomolecules within these assemblies from the composing protein sequences. Due to the scale of these systems, atomistic simulations would be severely limited in scope, thus motivating the development of appropriate coarse-grained models. Using coarse-grained molecular dynamics simulations, we are able to consistently model condensed and dilute phase properties of disordered proteins, and show that many of these sequences follow the behavior of homopolymers. Using these relations, we can predict phase behavior of protein sequences using simulations of a single chain.