Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils.

By A. Petkova, Wai-Ming Yau, R. Tycko. Biochemistry, 2006

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Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril (2016, background): “(2015) Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM.”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “In one model the protofilaments are 6 nm in width and associate laterally to form striated ribbons (82), whereas in the other model the protofilaments are 7 nm in width but do not associate laterally (72).”
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, methodology): “Solid state NMR data for striated ribbons, reported previously (4, 15), are significantly different from the corresponding data for twisted fibrils.”