Single-molecule tracking at scale, analyzing millions of cells and thousands of compounds per day, demonstrates that measuring protein motion provides mechanistic insights relevant to drug discovery.

Biophysical binding and structural prediction studies reveal that Tetraspanin12 directly binds the ligand Norrin, in a manner that is negatively cooperative with Norrin-Fzd4 binding and competitive with Norrin-LRP5/6 binding.

Single-molecule localization imaging shows that the Nipah virus fusion protein forms nanoscale clusters on cell and viral membranes that favor membrane fusion activation.

NMR and clustering results show that N-terminal acetylation of α-syn enhances its binding to the neutral phospholipid lysophosphatidylcholine, thereby promoting its function of clustering synaptic vesicles.

The Parkinson’s protein Leucine-Rich Repeat Kinase 2 contains a GTPase as well as kinase domain and modulates its intrinsic GTPase activity by autophosphorylation of the P-loop residue threonine 1343.