Uncovering molecular mechanisms in biomolecular assemblies linked to disease and health

Intrinsically disordered proteins (IDPs) can rapidly self-assemble into oligomers, liquid-liquid phase separation and insoluble aggregates. IDPs are both associated with maintaining cellular functions, and with diseases like ALS.

How specific protein structures and assemblies determine disease or health, and how it is involved in cellular regulation is not clear.

IDPs are difficult to study due to their dynamic, sticky, and transient nature, which makes it challenging to obtain high-resolution mechanistic data on the structure and dynamics of the assemblies.

Using mass spectrometry (MS)-based approaches I will resolve molecular interactions and complexes in two IDPs, CPEB3 and TDP43, under native-like conditions.

Native, IM-MS (size and conformation) and HDX-MS (structure) and molecular dynamics simulations will help achieve high-resolution structural features of complex assembly processes.

This strategy will uncover novel and transient interactions governing biological functions and molecular mechanisms linked to health and disease. My research lab, initially consisting of a PhD student and me (PI), will be set up at Stockholm University (SU). SU has leading expertise within protein folding and interactions.

My expertise in native and IM-MS of intact protein complexes complements the resourceful biophysics platform at SU.

My research on neuro-related IDPs, biomolecular complexes and MS method-development, perfectly matches and complements the ongoing research at SU.