“Chaperone-guided folding of nascent proteins”

Co-translational folding likely simplifies the conformational search problem for large proteins, but the events leading to correctly folded, functional structures remain poorly characterized. Domain-wise folding and help from chaperones are particularly important for multi-domain proteins, which constitute a large fraction of all proteomes. Using optical tweezers, we have dissected the folding of elongation factor G, a multi-domain protein that requires chaperones for folding. Our single-molecule studies reveal how interactions among domains affect folding and stability, and how interactions of the nascent protein with the ribosome and with molecular chaperones shape the folding pathway.

 

Prof Christian Kaiser

John Hopkins University