The ability of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) in proteins to self-associate is a vital mechanism for the formation of membrane-less organelles and cell structures. The self-association of IDPs play crucial roles in several cell functions, including immune response, genome organization, transcription, and neuronal signaling. On the other hand, several proteins that self-associate are also involved in neurological diseases, where they form toxic aggregates; these diseases include Alzheimer’s disease and Parkinson’s disease. The mechanisms behind IDP-mediated self-association still need to be better understood.

This is a continuation of the HALRIC project, which has been combining scattering and imaging techniques at European XFEL in a proof-of concept study with no established routines for processing and analyzing data. The results are expected to constitute a significant step towards deciphering the structure-function relationship of IDPs, which is vital for developing the next generations of pharmaceuticals, such as antibiotics, i.e., antimicrobial peptides. The latter aligns with the European Union’s sustainability goal for Agenda 2030. An expanded project team now wants to tune in on this data management of the large amount of data obtained in the HALRIC experiments with more extensive computer simulations at both LUNARC and the National Academic Infrastructure for Supercomputing in Sweden (NAISS).

For further information about this HALRIC pilot project, please contact:

Marie Skepö, Lund University
marie.skepo@compchem.lu.se