Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins.

ABSTRACT: The complex cellular milieu can spontaneously demix, or phase separate, in a process controlled in part by intrinsically disordered (ID) proteins. A protein's propensity to phase separate is thought to be driven by a preference for protein-protein over protein-solvent interactions. The hydrodynamic size of monomeric proteins, as quantified by the polymer scaling exponent (v), is driven by a similar balance. We hypothesized that mean v, as predicted by protein sequence, would be smaller for proteins with a strong propensity to phase separate. To test this hypothesis, we analyzed protein databases containing subsets of proteins that are folded, disordered, or disordered and known to spontaneously phase separate. We find that the phase-separating disordered proteins, on average, had lower cal

SUBMITTER: Paiz EA 

PROVIDER: S-EPMC8592878 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature