We study aberrant conformational transitions and pathological aggregation of disease-associated proteins, with an emphasis on proteins implicated in neurodegenerative disorders and additional work on aggregation associated with cancer and metabolic disease. We investigate how mutations, key structural motifs, and environmental factors regulate misfolding, oligomerization, nucleation, and amyloid fibril formation. We also examine the structural polymorphism of aggregates, their interactions with biological membranes, and the resulting membrane damage.
