This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

As our understanding of the molecular structures of amyloid fibrils has matured over the past
15 years, it has become clear that, while amyloid fibrils do have well‐defined molecular …

The cross-β amyloid form of peptides and proteins represents an archetypal and widely
accessible structure consisting of ordered arrays of β-sheet filaments. These complex …

Polyglutamine expansion within the exon1 of huntingtin leads to protein misfolding,
aggregation, and cytotoxicity in Huntington's disease. This incurable neurodegenerative …

A long-standing goal of amyloid research has been to characterize the structural basis of the
rate-determining nucleating event. However, the ephemeral nature of nucleation has made …

Polyglutamine (polyQ) sequences of unknown normal function are present in a significant
number of proteins, and their repeat expansion is associated with a number of genetic …

We structurally compare, using solid-state NMR, two different polymorphs of α-synuclein
which, as established recently, display contrasting biochemical properties, toxicity, and …

Neurodegeneration in Huntington's disease (HD) is accompanied by the aggregation of
fragments of the mutant huntingtin protein, a biomarker of disease progression. A particular …

Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural
characterization of a diverse array of biological assemblies that include amyloid fibrils, non …

Polyglutamine expansion in the huntingtin protein is the primary genetic cause of
Huntington's disease (HD). Fragments coinciding with mutant huntingtin exon1 aggregate in …