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George Rose Lab
The George Rose Lab investigates protein folding, the spontaneous disorder transition that takes place under physiological conditions. The protein polymer is flexible in its unfolded state but takes on a unique native, three-dimensional form when folded. We propose that the folded state is selected from a set number of structural possibilities, each corresponding to either a distinct hydrogen-bonded arrangement of ??helices or a strand of ??sheet.
Herschel Wade Lab
The emergence of structural genomics, proteomics and the large-scale sequencing of many genomes provides experimental access to regions of protein sequence-structure-function landscapes which have not been explored through traditional biochemical methods. Protein structure-function relationships can now be examined rigorously through the characterization of protein ensembles, which display structurally convergent--divergent solutions to analogous or very similar functional properties.
In this modern biochemical context, the Herschel Wade Lab will use protein libraries, chemistry, biophysics, molecular biology and structural methods to examine the basis of molecular recognition in the context of several important biological problems, including structural and mechanistic aspects of multi-drug resistance, ligand-dependent molecular switches and metal ion homeostasis.