<p>Single-molecule force spectroscopy (SMFS) enables high-resolution insights into the kinetics and mechanisms of biomolecular interactions. In this talk, I will present how SMFS, helps uncover key principles in nucleic acid and protein folding. Examples discussed will include the microsecond invasion kinetics of toehold-mediated strand displacement (TMSD) of DNA and RNA as well as mRNA-Roquin interactions, which regulate mRNA degradation via specific 3’UTR hairpin structures. Finally, we study chaperone-mediated unfolding of the glucocorticoid receptor (GR), demonstrating how Hsp70/Hsp40 unfolds GR in discrete ATP-driven steps, stabilizing novel intermediates and acting as an unfoldase. These studies showcase SMFS as a powerful tool to resolve biomolecular dynamics providing new insights into RNA structure-function relationships and chaperone-mediated protein regulation.</p>
