Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

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 …

All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from
proteins associated with different diseases remains unclear. Here, we combine cryo-EM and …

Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human
diseases. Recent advances in electron microscopy and solid state NMR have allowed the …

Amyloid disorders cause debilitating illnesses through the formation of toxic protein
aggregates. The mechanisms of amyloid toxicity and the nature of species responsible for …

Protein therapeutics carry inherent limitations of membrane impermeability and structural
instability, despite their predominant role in the modern pharmaceutical market. Effective …

The presence of amyloid plaques composed of amyloid beta (Aβ) fibrils is a hallmark of
Alzheimer's disease (AD). The Aβ peptide is present as several length variants with two …

Solid-state nuclear magnetic resonance (ssNMR) is indispensable for studying the
structures, dynamics, and interactions of insoluble proteins in native or native-like …

The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the
micrometer and molecular scales. Various fibril growth conditions have been identified to …