Protein Folding: Chaperone Solutions

This lecture explores the role of chaperones in guiding protein folding, focusing on the functional cycle of Hsp70 and the DnaK chaperone system. It delves into the slow folding of Fluc in the absence of chaperones, the compact intermediates revealed by spFRET, and the rescue of misfolded proteins. The speaker discusses the chaperonin-mediated folding of actin, the structural dynamics of chaperonin-bound actin, and the nucleotide-driven conformational cycle. Special properties of TRiC, a heterooligomeric chaperonin, are highlighted, along with the completion of actin folding in the TRiC cavity. The lecture concludes with insights into how chaperones actively remodel the folding energy landscape, emphasizing their role in preventing protein misfolding.