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||P.324 right column bottom paragraph: "Protein Folding and Aggregation: The folded three-dimensional structures of most proteins represent a compromise between thermodynamic stability and the conformational flexibility required for function. Consequently, proteins are often marginally stable in their physiological environment and thus susceptible to misfolding and aggregation (refs 2, 3). In addition, a substantial fraction of proteins in eukaryotic cells (∼30%) are classified as intrinsically unstructured and contain regions thought to adopt ordered structure only upon interaction with binding partners (primary source). Such proteins may be metastable and prone to aggregation."