Sequence-Dependent Material Properties of Biomolecular Codensates and their Relation to Dilute Phase Conformations.

ABSTRACT: Material properties of phase-separated biomolecular assemblies, enriched with disordered proteins, dictate their ability to participate in many cellular functions. Despite the significant effort dedicated to understanding how the sequence of the disordered protein drives its phase separation to form condensates, little is known about the sequence determinants of condensate material properties. Here, we computationally decipher these relationships for charged disordered proteins using model sequences comprised of glutamic acid and lysine residues as well as naturally occurring sequences of LAF1's RGG domain and DDX4's N-terminal domain. We do so by delineating how the arrangement of oppositely charged residues within these sequences influences the dynamical, rheological, and interfacial pro

SUBMITTER: Devarajan DS 

PROVIDER: S-EPMC10197689 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature