Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …

The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

Alzheimer's disease is the most common neurodegenerative disease, and there are no
mechanism-based therapies. The disease is defined by the presence of abundant …

Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common
properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and …

Prion diseases are caused by the misfolding of prion protein (PrP). Misfolded PrP forms
protease-resistant aggregates in vivo (PrPSc) that are able to template the conversion of the …

The discovery of infectious proteins, denoted prions, was unexpected. After much debate
over the chemical basis of heredity, resolution of this issue began with the discovery that …

Current interest in amyloid fibrils stems from their involvement in neurodegenerative and
other diseases and from their role as an alternative structural state for many peptides and …

Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some
amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative …

We describe solid-state nuclear magnetic resonance (NMR) measurements on fibrils formed
by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1-40) that …

Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional
structure, which is therefore of paramount importance for the prion function. However, no …