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Capturing denaturing proteins – Small Heat Shock Protein substrate recognition Elizabeth Vierling and Indu Santhanagopalan Protein aggregation resulting from stress, disease or mutation poses a major threat to all cells. The ubiquitous small heat shock proteins (sHSPs) act as molecular chaperones to prevent irreversible protein aggregation and are significant components of the protein quality control network. Expression and/or mutation of sHSPs are linked to multiple diseases of protein misfolding, including neurodegenerative diseases, myopathies and cataract. The mechanism of sHSP chaperone action and interaction with substrates, therefore, has wide-ranging implications for understanding cellular stress and disease processes. We are studying the mechanism of sHSP substrate recognition by identifying specific crosslinking sites between sHSPs and denaturing substrates. sHSPs are oligomeric proteins of 12 to > 24 subunits, which readily dissociate to bind up to an equal weight of denaturing proteins. Substrates in these large, soluble and heterogenous sHSP-substrate complexes are later released and refolded by ATP-dependent chaperones. Pinpointing sHSP:substrate interaction sites, as well as determining the overall organization of the these complexes, is critical to understanding how they carry out their chaperone function.