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Molecular chaperones are necessary for maintaining a functional proteome in the cell by preventing the aggregation of unfolded proteins and/or assisting with their folding. Despite the central importance of the binding of chaperones to unfolded substrates, the structural basis of their interaction remains poorly understood. The scarcity of structural data on complexes between chaperones and unfolded client proteins is primarily due to technical challenges originating in the dynamic nature of these complexes.
I will discuss how NMR spectroscopy can be used as an extremely powerful tool to determine the structural and dynamic basis for the recognition and interaction of unfolded proteins by molecular chaperones.