Magic angle spinning (MAS) NMR studies of amyloid and membrane proteins and large
macromolecular complexes are an important new approach to structural biology. However …

Amyloid-β (Aβ) is a 39–42 residue protein produced by the cleavage of the amyloid
precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that …

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 …

Supramolecular chemistry provides structural and conformational information about
complexes formed from multiple molecules. While the molecule is held together by strong …

We describe magic-angle spinning NMR experiments designed to elucidate the interstrand
architecture of amyloid fibrils. Three methods are introduced for this purpose, two being …

The aggregation of proteins and peptides into a variety of insoluble, and often non-native,
aggregated states plays a central role in many devastating diseases. Analogous processes …

Protein magic angle spinning (MAS) NMR spectroscopy has generated structural models of
several amyloid fibril systems, thus providing valuable information regarding the forces and …

Amyloid fibrils are ordered, insoluble protein aggregates that are associated with
neurodegenerative conditions such as Alzheimer's disease. The fibrils have a common rod …

Magic angle spinning (MAS) nuclear magnetic resonance (NMR) has evolved significantly
over the past three decades and established itself as a vital tool for the structural analysis of …

Several human diseases are associated with the formation of amyloid aggregates, but
experimental characterization of these amyloid fibrils and their oligomeric precursors has …