From globular proteins to amyloids
Proposes a model and mechanism for explaining protein misfolding. Concepts presented are based on a model originally intended to show how proteins attain their native conformations. This model is quantitative in nature and founded upon arguments derived from information theory. It facilitates prediction and simulation of the amyloid fibrillation process, also identifying the progressive changes that occur in native proteins that lead to the emergence of amyloid aggregations. Introduces basic rules for protein folding, along with the conditions that result in misfolding Presents research that lies in treating the aqueous environment as a continuum rather than a set of individual water molecules (i.e. the classic representation) Provides practical applications for helping the prevention of amyloidosis and improving drug design
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