Intrinsically disordered protein regions (IDRs) play a key role in the formation of biomolecular condensates, but details of the underlying mechanism at the microscopic level remain at the center of ongoing studies. Here, the authors use microsecond-level molecular dynamics simulations and fractal formalism to study a model dense phase composed of 24 copies of a C-terminal 73- residue arginine- and glycine-rich IDR (RGG3) of fused in sarcoma (FUS) in the absence of RNA with atomistic resolution, showing that RGG3 exhibits a distinct dynamic binding mode with statistically defined interaction motifs and a robust multi-scale topology of self-associated protein clusters.
- Anton A. Polyansky
- Benjamin Frühbauer
- Bojan Žagrović
