Explores the selective promiscuity in binding of the E. coli Hsp70 chaperone to unfolded or misfolded protein substrates, examining its implications in protein folding mechanisms.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores beta-hairpins in polyglutamine protein aggregation, focusing on Huntington's disease and the molecular mechanisms behind toxic fibril formation.
Explores deciphering protein interaction fingerprints using geometric deep learning and the challenges in computational protein-protein interaction design.
Explores protein aggregation in neurodegenerative diseases, emphasizing the need to rethink treatment strategies and understand the role of post-translational modifications.