Molecular chaperones are essential for maintaining protein homeostasis by assisting the folding of nascent and misfolded proteins into their functional conformations. Our research focuses on the Hsp60/Hsp10 chaperone system and seeks to understand the molecular mechanisms that govern its protein folding cycle. Although Hsp60 is one of the most highly conserved and essential chaperones across bacteria, yeast, and mammals, many aspects of how it recognizes, encapsulates, and remodels substrate proteins remain poorly understood. To address these questions, we employ a combination of biochemical and biophysical approaches, with a particular emphasis on solution-state NMR spectroscopy and cryo-electron microscopy. These studies will provide fundamental insights into the dynamic conformational changes and substrate interactions that drive chaperone-assisted protein folding, advancing our understanding of a central process in cellular proteostasis.