Thermodynamic forces from protein and water govern condensate formation of an intrinsically disordered protein domain.

ABSTRACT: Liquid-liquid phase separation (LLPS) can drive a multitude of cellular processes by compartmentalizing biological cells via the formation of dense liquid biomolecular condensates, which can function as membraneless organelles. Despite its importance, the molecular-level understanding of the underlying thermodynamics of this process remains incomplete. In this study, we use atomistic molecular dynamics simulations of the low complexity domain (LCD) of human fused in sarcoma (FUS) protein to investigate the contributions of water and protein molecules to the free energy changes that govern LLPS. Both protein and water components are found to have comparably sizeable thermodynamic contributions to the formation of FUS condensates. Moreover, we quantify the counteracting effects of water mole

SUBMITTER: Mukherjee S 

PROVIDER: S-EPMC10514047 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature