Roshan Mammen Regy

TL;DR: This work explores a model protein, the disordered N-terminal domain of LAF-1, and highlights how three key features of the sequence control the protein’s propensity to phase-separate, and identifies a region of the RGG domain that has high contact probability and is highly conserved between species; deletion of this region significantly disrupts phase separation in vitro and in vivo.

TL;DR: The simulation approach presented here allows the structural and dynamical properties of biomolecular condensates to be studied in microscopic detail and is generally applicable to single- and multicomponent systems of proteins and nucleic acids involved in LLPS.

TL;DR: A coarse-grained polynucleotide model is developed which together with the recently developed HPS model for protein LLPS, allows to capture the factors driving protein-polynucleotide phase separation and explores the role of charge patterning on controlling polyn nucleotide incorporation into condensates.

TL;DR: A novel multiscale computational framework is presented by obtaining initial molecular configurations of a condensed protein-rich phase from equilibrium coarse-grained simulations, and back mapping to an all-atom representation, and demonstrating that the proteins are remarkably dynamic within the condensed phase.

TL;DR: In this article, the hydropathy scale (HPS) coarse-grained (CG) model is used to simulate sequence-specific behavior of intrinsically disordered proteins (IDPs), including their liquid-liquid phase separation (LLPS).