Structure and Dynamics of Intrinsically Disordered Proteins

The importance of disorder in protein structure and function is becoming increasingly evident. However the computational model able to quantitatively capture the structure and dynamics of the intrinsically disordered proteins (IDPs) is still challenging due to the very broad distribution of protein conformations. We are actively developing computational models for IDPs in multiple resolutions, including all-atom, coarse-grained and polymer models. In this talk I will present our coarse-grained models to investigate how IDPs undergo liquid-liquid phase separation and form dynamic assemblies. These assemblies behave like liquid droplets and are closely related to the formation of membraneless organelles and pathological aggregates. Our main effort has been directed toward understanding the molecular mechanisms of the phase behavior and how we can predict the phase boundaries from the composing IDP sequences. Here we find 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.