Biochemists simulate a protein-folding chaperone's functional dance
Gierasch says, "This one presented us with quite a scientific challenge, because all the techniques we usually use to look at communication between the different domains in proteins get stuck when the targets are flexible and not rigid, and the interdomain linker in Hsp70s is very flexible. We had to be clever in our approach." Details are in the Journal of Biological Chemistry . As she explains, heat shock proteins in the Hsp70 family - molecular weight 70 - are "a really important class of molecular chaperones that have many important jobs in the cell, including binding to client proteins to assist their folding, or to keep them from pathologically aggregating, or to keep them unfolded so they can pass threadlike through a membrane." She describes the three parts of a folded Hsp70 protein as a nucleotide -binding domain and substrate-binding domain linked by a "mysterious" interdomain linker, which becomes part of the structure when a small molec...