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The cornerstone of structural biology is the unique relationship betweenprotein sequence and the 3D structure at equilibrium. Although intrinsicallydisordered proteins (IDPs) do not fold into a specific 3D structure, breakingthis paradigm, some IDPs exhibit large-scale organization, such asliquid-liquid phase separation. In such cases, the structural plasticity hasthe potential to form numerous self-assembled structures out of thermalequilibrium. Here, we report that high-temperature incubation time is adefining parameter for micro and nanoscale self-assembly of resilin-like IDPs.Interestingly, high-resolution scanning electron microscopy micrographs revealthat an extended incubation time leads to the formation of micron-size rods andellipsoids that depend on the amino acid sequence. More surprisingly, aprolonged incubation time also induces amino acid composition-dependentformation of short-range nanoscale order, such as periodic lamellarnanostructures. We, therefore, suggest that regulating the period ofhigh-temperature incubation, in the one-phase regime, can serve as a uniquemethod of controlling the hierarchical self-assembly mechanism of structurallydisordered proteins.

Modulating Hierarchical Self-Assembly In Thermoresponsive Intrinsically Disordered Proteins Through High-Temperature Incubation Time