The phase separation of disordered proteins resulting in the formation of biomolecular condensates has received significant attention due to its fundamental role in cellular organization and functioning, and is sought after in many applications. For instance, the liquid-liquid phase separation of tropoelastin initiates the hierarchical assembly of elastic fibers—key components of the extracellular matrix providing resilience and elasticity to biological tissues. Inspired by the hydrophobic domains (HDs) of tropoelastin, elastin-like polypeptides (ELPs) were derived, exhibiting a similar phase behavior. Employing state-of-the-art atomistic modeling, I will demonstrate the importance of the sequence length as a modulator of conformational properties at a single chain level, manifesting in different aggregate states of elastin condensates. Next, I will show that disordered proteins can behave as entirely different polymers, i.e., coils and globules, in different regions of their free-energy landscape, using beta-casein as an example. Finally, I will discuss how to reach large-scale assemblies of IDPs by employing the Martini force field.
Tatiana I. Morozova (Sun,) studied this question.