Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range.

ABSTRACT: The formation and viscoelastic properties of condensates of intrinsically disordered proteins (IDPs) is dictated by amino acid sequence and solution conditions. Because of the involvement of biomolecular condensates in cell physiology and disease, advancing our understanding of the relationship between protein sequence and phase separation (PS) may have important implications in the formulation of new therapeutic hypotheses. Here, we present CALVADOS 2, a coarse-grained model of IDPs that accurately predicts conformational properties and propensities to undergo PS for diverse sequences and solution conditions. In particular, we systematically study the effect of varying the range of the nonionic interactions and use our findings to improve the temperature scale of the model. We further opt

SUBMITTER: Tesei G 

PROVIDER: S-EPMC10450847 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature