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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.
Delves into the contrasting effects of chaperones on amyloid beta peptide aggregation, exploring inhibitors, oligomer quantification, and antibody impacts.
Explores the importance of protein-ligand interactions, focusing on binding affinities and energetic landscapes, with implications for drug development and specificity.
