Mechanisms of chaperone-assisted protein folding
A large fraction of newly synthesized proteins in the cell require assistance of molecular chaperones to reach their native folded states efficiently. Our goal is the complete understanding of how the chaperone machinery affects complex folding energy landscape, by preventing aggregation, accelerating folding or maintaining them in a folded or “folding-competent” state. Using biophysical tools taken from studies of well-defined single domain proteins, NMR, computational and biochemical methods, we would like to characterize the structures, energetics and conformational changes occurring at every stage of chaperone-assisted protein folding, from the nascent chain stage to the complete, fully folded protein.
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