Hsp70 Chaperone Binding: Substrate Selectivity and Function

This lecture explores the selective promiscuity in binding of the E. coli Hsp70 chaperone to unfolded or misfolded protein substrates. The instructor discusses the binding nature, preferred sites, and the relationship to Hsp70 functions. Various functions, such as folding, hand-off to downstream chaperones, and disassembly processes, are examined. The lecture delves into the binding behavior of DnaK to a protein substrate, the structural aspects of substrate binding, and the implications of Hsp70 binding preferences in protein folding mechanisms. The study of peptide binding to the substrate-binding domain (SBD) and the conformational rearrangements during binding are also highlighted.