Nevertheless, our understanding of IDPs and their key role in mediating phase separations of multicomponent structures into coacervate assemblies is still largely limited. In the literature, mean-field theories such as Flory-Huggins theory and a recently emerging sticker-and-spacer model provide highly generalizable frameworks for describing the thermodynamics of the phase behavior of associate polymers in solution , with emerging applications to complex biological systems both experimentally and computationally . The thermodynamic driving force towards phase separation is likely to be inherently determined by the conformational free energy (FE) landscape of individual IDPs (intramolecular factor) and their molecular interactions with other sequences in solution including their own replicates (intermolecular factor). Thus, uncovering protein dynamics and their structure-function relationship can be pivotal for establishing versatile and sensitive protocols to design, program and predict the bottom-up assembly of multifunctional bio-inspired proteinbased materials based on IDPs.