Chapter 9: Studying Molecular Chaperones and Their Client Interactions by Nanometer Distance Restraints from Electron Paramagnetic Resonance Spectroscopy

The fundamental task of de novo protein folding and refolding is ensured by the diverse family of molecular chaperones. Insight into the structure, conformational changes and client interactions is key to understanding the processes within the complex chaperone network. Electron paramagnetic resonance (EPR) spectroscopy combined with site-directed spin labeling (SDSL) is a suitable technique to unravel the processes involving chaperone activity. In this chapter, we review the state-of-the-art SDSL-EPR methodology, in particular distance determination providing structural information. Recent work in the field of molecular chaperones studied by EPR spectroscopy is summarized illustrating the tremendous potential and versatile applicability of this method.