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Probing Protein–Chaperone Interactions with Single-Molecule Fluorescence Spectroscopy


  • We thank A. Szabo for discussions and advice on anisotropy simulations, A. Plückthun and M. Kawe for discussions and samples of GroEL, H. Hofmann and D. Streich for discussions, the late P. Horowitz for a plasmid encoding rhodanese, and G. Lorimer for a plasmid encoding SR1. This work was supported by the VolkswagenStiftung, the Schweizerische Nationalfonds, the Swiss National Center of Competence in Research for Structural Biology, and the Human Frontier Science Program.


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Molecular chaperones aid protein folding in the cell, but their effects on the conformation of the substrate protein have largely eluded experimental investigation. Single-molecule fluorescence spectroscopy was used to extract structural and dynamic information from a protein–chaperone complex (see figure; yellow: rhodanase, blue: GroEL). This approach will aid in a more physical understanding of the role of cellular factors in protein folding.