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This lecture by Sebastian Hiller explores the dynamic interactions between molecular chaperones and client proteins at an atomic resolution. The discussion covers the definition of molecular chaperones, their role in protein homeostasis, key open questions regarding chaperone-client interactions, and various approaches to studying chaperone structures. The lecture delves into the specific case of the chaperone Skp and its role in membrane protein transport in Gram-negative bacteria. It also examines the structural dynamics of the Trigger Factor dimer and the impact of chaperones on a-Synuclein, a protein central to Parkinson's disease. The presentation concludes with insights into the mechanisms of chaperone-a-Synuclein homeostasis.