Modulating hierarchical self-assembly in thermoresponsive intrinsically disordered proteins through high-temperature incubation timeAbstract

TitleModulating hierarchical self-assembly in thermoresponsive intrinsically disordered proteins through high-temperature incubation timeAbstract
Publication TypeJournal Article
Year of Publication2023
AuthorsSethi, V, Cohen-Gerassi, D, Meir, S, Ney, M, Shmidov, Y, Koren, G, Adler-Abramovich, L, Chilkoti, A, Beck, R
JournalScientific Reports
Volume13
Issue1
Date Published11/2023
Abstract

The cornerstone of structural biology is the unique relationship between protein sequence and the 3D structure at equilibrium. Although intrinsically disordered proteins (IDPs) do not fold into a specific 3D structure, breaking this paradigm, some IDPs exhibit large-scale organization, such as liquid–liquid phase separation. In such cases, the structural plasticity has the potential to form numerous self-assembled structures out of thermal equilibrium. Here, we report that high-temperature incubation time is a defining parameter for micro and nanoscale self-assembly of resilin-like IDPs. Interestingly, high-resolution scanning electron microscopy micrographs reveal that an extended incubation time leads to the formation of micron-size rods and ellipsoids that depend on the amino acid sequence. More surprisingly, a prolonged incubation time also induces amino acid composition-dependent formation of short-range nanoscale order, such as periodic lamellar nanostructures. We, therefore, suggest that regulating the period of high-temperature incubation, in the one-phase regime, can serve as a unique method of controlling the hierarchical self-assembly mechanism of structurally disordered proteins.

URLhttps://www.nature.com/articles/s41598-023-48483-w
DOI10.1038/s41598-023-48483-w
Short TitleSci Rep