Unraveling the Kinetic Mechanism of the 70-kDa Molecular Chaperones Using Fluorescence Spectroscopic Methods

This article reviews the recent progress in unraveling the kinetic mechanism of the 70-kDa molecular chaperones by the use of fluorescence spectroscopic methods. Dissecting the kinetics of the individual steps in the 70-kDa chaperone reaction cycle in vitro—ATP binding, peptide binding, interdomain coupling, and chaperone-catalyzed ATP hydrolysis—provides a foundation which can be used to develop a clear understanding of the molecular basis for chaperone activity in vivo.