Phase behavior of biopolymers, such as spontaneous organization of intrinsically disordered proteins (IDP) into membraneless organelles or droplets, could be explained by considering equilibrium thermodynamics. Our simulation study reveals that the IDP α-synuclein, in equilibrium conditions, assembles into percolated structures with the characteristic of microphase separation, in contrast to the commonly hypothesized mechanism of a simple liquid-liquid phase separation. This opens a new paradigm to understand the birth and structure of membraneless organelles.

Understanding the effect of non-equilibrium fluctuations on polymer conformations is also important from both biological and material science perspective. In this aspect, using minimal model of polymers under active fluctuations, we discover that the coil-to-globule transition still holds with an impact on the solvent quality due to the active forces. Further, we observe that even small amounts of activity, when aligned along the backbone of a stiff polymer, leads to an ensemble of dynamic conformations under confinement, usually identified as glassy metastable states. Thus, overall, we get an outlook of plausible structural reorganization in self-assembling biological or synthesized polymeric systems arising from a combined interplay of thermal, dispersive and active forces.