A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR.

By A. Petkova, Y. Ishii, J. Balbach, O. Antzutkin, Richard Leapman, Frank Delaglio, R. Tycko. Proceedings of the National Academy of Sciences of the United States of America, 2002

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FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils (2004, methodology): “The presently available NMR data on the structure of amyloid fibrils lead to twist angles of 26° ± 24° for TTR(105–115) fibrils, and 14° ± 37°, as well as 17° ± 38° for the two data sets of A (1–40) (Petkova et al. 2002).”
Endoplasmic reticulum stress signaling in disease. (2006, background): “In contrast, amyloid can be formed through polymerization of a number of otherwise unrelated proteins, each causing a distinct disease (79, 148, 207).”
Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. (2006, methodology): “Residues 1-8 are omitted, as these residues are known to be structurally disordered from solid state NMR linewidth data (10, 11), measurements of intermolecular 13C-13C dipole-dipole couplings (37, 38), hydrogen exchange data (26, 27), and proteolysis data (61, 62).”
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, unknown): “Aβ1-40 β 1: 12–24 17–22 [78] β 2: 30–40 30–40”