Protein folding amyloid aggregates

The lessons we have learned from physics are of a different nature. The history of physics is replete with examples of the elucidation of connections between what seem to be distinct phenomena and the development of a unifying framework, which, in turn, leads to new observable consequences [13]. Indeed, strong evidence suggests that globular proteins share many common characteristics their ability to fold rapidly and reproducibly in order to create a hydrophobic core, the fact that there seem to be a relatively small number (on the order of a few thousand) of distinct modular folds made up of helices and almost planar sheets, the fact that protein folds are flexible and versatile in order to accomplish the dizzying array of functionalities that these proteins perform, and the unfortunate tendency of proteins to aggregate and form amyloids, which are implicated in human diseases. 

S. E. Radford and C. M. Dobson. From computer simulations to human disease emerging themes in protein folding. Cell, 97 (1999), 291 M. Bucciantini, E. Giannoni, F. Chiti et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature, 416 (2002), 507 M. Dumoulin, A. M. Last, A. Desmyter et al. A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature, 424 (2003), 783 F. Chiti, M.Stefani,... 

Protein Folding Disorders. - There are twenty five or so known proteins that can misfold and aggregate into fibrils. Of these, three are glycosylated the amyloid associated membrane protein (AAP) in Alzheimer s the prion in scrapie. 

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