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Probing Protein–Chaperone Interactions with Single‐Molecule Fluorescence Spectroscopy
Author(s) -
Hillger Frank,
Hänni Dominik,
Nettels Daniel,
Geister Sonja,
Grandin Michelle,
Textor Marcus,
Schuler Benjamin
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200800298
Subject(s) - groel , chaperone (clinical) , protein folding , biophysics , single molecule experiment , force spectroscopy , fluorescence , fluorescence spectroscopy , chemistry , single molecule fret , molecule , folding (dsp implementation) , spectroscopy , förster resonance energy transfer , crystallography , biochemistry , biology , physics , medicine , organic chemistry , pathology , escherichia coli , quantum mechanics , electrical engineering , gene , engineering
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.