Explores proteostasis regulation through chaperone interactions and post-translational modifications, revealing insights into protein quality control mechanisms.
Explores the evolution and function of protein-repair machineries, emphasizing the role of ATP-fueled unfolding machines in preventing protein aggregation and promoting proper folding.
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 importance of protein-ligand interactions, focusing on binding affinities and energetic landscapes, with implications for drug development and specificity.
