Huntington disease is devastating to patients and their families—with autosomal dominant
inheritance, onset typically in the prime of adult life, progressive course, and a combination of …

In Huntington's Disease and related expanded CAG repeat diseases, a polyglutamine [poly(Gln)]
sequence containing 36 repeats in the corresponding disease protein is benign, …

Long glutamine sequences (polyQ) occur in many cell proteins, and several neurodegenerative
diseases result from expansion of these sequences. PolyQ-containing proteins are …

Over residues 15–36, which comprise the H-bonded core of the amyloid fibrils it forms, the
Alzheimer's disease plaque peptide amyloid β (Aβ) possesses a very similar sequence to that …

Simple polyglutamine (polyQ) peptides aggregate in vitro via a nucleated growth pathway
directly yielding amyloid-like aggregates. We show here that the 17-amino-acid flanking …

Although the amyloid fibrils formed from the Alzheimer's disease amyloid peptide Aβ are
rich in cross-β sheet, the peptide likely also exhibits turn and unstructured regions when it …

A number of observations point to the aggregation of expanded polyglutamine [poly(Q)]-containing
proteins as playing a central role in the etiology of Huntington's disease (HD) and …

Amyloid formation reactions exhibit two classes of polymorphisms: the metastable intermediates
commonly observed during amyloid formation and the range of conformationally distinct …

The Alzheimer's amyloid peptide A β(1 – 40) generates a turbid, Congo red-binding aggregation
reaction product within minutes when incubated in the pH range 5 to 6. At pH 7.4, A β …

Disease-related amyloid fibrils appear to share a common, but poorly understood, structure.
We describe here the generation and preliminary characterization of two conformation-…