The discovery of Intrinsically Disordered Proteins, which contain significant levels of disorder
yet perform complex biologically functions, as well as unwanted aggregation, has motivated …

The post-translational conversion of the ubiquitously expressed cellular form of the prion
protein, PrPC, into its misfolded and pathogenic isoform, known as prion or PrPSc, plays a …

The propensity of protein molecules to self-assemble into highly ordered, fibrillar aggregates
lies at the heart of understanding many disorders ranging from Alzheimer's disease to …

Secondary structure assignment codes were built to explore the regularities associated with
the periodic motifs of proteins, such as those in backbone dihedral angles or in hydrogen …

The development of transmissible spongiform encephalopathies (TSEs) is associated with
the conversion of the cellular prion protein (PrPC) into a misfolded, pathogenic isoform …

The misfolding of proteins into amyloid fibrils constitutes the hallmark of many diseases.[1]
Although relatively few physicochemical properties of protein sequences—charge …

Amyloid formation involves the conversion of soluble protein species to an aggregated state.
Amyloid fibrils of β-parvalbumin, a protein abundant in fish, act as an allergen but also inhibit …

Methionine/valine polymorphism at position 129 of the human prion protein, huPrP, is tightly
associated with the pathogenic phenotype, disease progress, and age of onset of …

The partial unfolding of human lysozyme underlies its conversion from the soluble state into
amyloid fibrils observed in a fatal hereditary form of systemic amyloidosis. To understand the …

Prion diseases, like Alzheimer's disease and Parkinson disease, are rapidly progressive
neurodegenerative disorders caused by misfolding followed by aggregation and …