Publications
2026
- In prep.
- In prep.In preparation, 2026
- bioRxivbioRxiv, 2026
Explicit-solvent, near-atomic resolution coarse-grained simulations demonstrate how the interplay among different domains drives phase separation of full-length TDP-43. The simulations capture how the secondary structure of a conserved helix in the low-complexity domain (LCD) modulates phase separation and follow the effect of phosphomimicking mutations on condensation. Together with in vitro experiments, the work emphasizes the importance of the aromatic residues in the LCD as well as N-terminal residues 1-101 (including the NTD) for full-length TDP-43 condensation, and shows how specific NTD-NTD dimer formation modulates the phase behavior and the dynamic and interfacial properties of the condensates.