Relation between single-molecule properties and phase behavior of intrinsically disordered proteins.

ABSTRACT: Proteins that undergo liquid-liquid phase separation (LLPS) have been shown to play a critical role in many physiological functions through formation of condensed liquid-like assemblies that function as membraneless organelles within biological systems. To understand how different proteins may contribute differently to these assemblies and their functions, it is important to understand the molecular driving forces of phase separation and characterize their phase boundaries and material properties. Experimental studies have shown that intrinsically disordered regions of these proteins are a major driving force, as many of them undergo LLPS in isolation. Previous work on polymer solution phase behavior suggests a potential correspondence between intramolecular and intermolecular interactions

SUBMITTER: Dignon GL 

PROVIDER: S-EPMC6176625 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature