Rasmus K. Norrild

This study uses systematic K-to-Q mutagenesis to probe the energy landscape of α-Synuclein aggregation, identifying core residue mutations that alter free energy pathways and fibril polymorphism.

This study develops a high-throughput method to quantify interactions driving condensate formation in intrinsically disordered proteins and shows amino acid content primarily determines partitioning behavior.

This study shows that the thermodynamic stability of alpha-synuclein fibrils affects their disaggregation by the chaperone system HSP70, DNAJB1, and Apg2, with more stable fibrils being less efficiently disaggregated.