In the future, simulations will increasingly account for the fact that condensates in cells are constantly reshaped and can be out of equilibrium, e.g., due to the dissipation of a chemical fuel such as ATP. For example, enzymes can add post-translational modifications to proteins in condensates, modulating their behavior . Alternatively, systems can be out of equilibrium in that they have not (yet) reached the thermodynamically most favorable state. For instance, fibrillar structures are the most stable states for the IDRs of FUS and hnRNPA1 . With the current advances in molecular simulations, such complex systems and processes can be researched at an increasing level of detail and accuracy to decipher how structure, dynamics, and thermodynamic driving forces are linked to biological functions. authors show how sequences can be designed that give rise to maximally dynamic condensates.