TY - JOUR TI - High-resolution NMR spectroscopy of the β-amyloid(1-28) fibril typical for Alzheimer's disease AU - Mikros, E. AU - Benaki, D. AU - Humpfer, E. AU - Spraul, M. AU - Loukas, S. AU - Stassinopoulou, C.I. AU - Pelecanou, M. JO - Angewandte Chemie. International Edition PY - 2001 VL - 40 TODO - 19 SP - 3603-3605 PB - SN - 1433-7851, 1521-3773 TODO - 10.1002/1521-3773(20011001)40:19<3603::AID-ANIE3603>3.0.CO;2-5 TODO - Nuclear magnetic resonance spectroscopy, Fibrils, Diseases, amyloid beta protein, Alzheimer disease; article; beta sheet; nuclear magnetic resonance spectroscopy; nuclear Overhauser effect; protein analysis; protein assembly; protein structure; X ray crystallography TODO - Unlabeled samples of the β-amyloid peptide(1-28) fibrils typical of Alzheimer's disease could be used to obtain well-resolved one- and two-dimensional 1H NMR spectra (see picture). The technique applied was high-resolution magic-angle spinning on a 600 MHz NMR spectrometer. The results are in agreement with a parallel, in-register arrangement of the β-amyloid peptide in the fibril. ER -