TDP-43 is a protein which acts in part like an editor and in part like a postman; he modifies his "messages" written in RNA, before delivering them to the cytoplasm. Under certain "bad weather" conditions, part of the TDP-43 protein acts like an "umbrella" (really a hydrogel or functional amyloid) to protect the messages. But sometimes these "umbrellas" can break and become tangled together, forming a "net" (harmful amyloid aggregates) that disrupts the message editing and delivery system, and putatively leads to cell death. In fact, TDP-43 aggregates are linked to amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease that kills 4000 Spaniards per year. The elucidation by NMR of the structure, dynamics and stability of the first quarter, or N-terminal domain, of the TDP-43 protein's structure, dynamics and stability by NMR methods provides the keys to better understand the function and malfunction of this important protein.

Mompeán M, Romano V, Pantoja-Uceda D, Stuani C, Baralle FE, Buratti E and Laurents DV "The TDP-43 N-Terminal Domain Structure at High Resolution." FEBS J. Jan 12th, 2016
doi: 10.1111/febs.13651