@article{2982073,
    title = "High-resolution NMR spectroscopy of the β-amyloid(1-28) fibril typical for Alzheimer's disease",
    author = "Mikros, E. and Benaki, D. and Humpfer, E. and Spraul, M. and Loukas, S. and Stassinopoulou, C.I. and Pelecanou, M.",
    journal = "Angewandte Chemie.  International Edition",
    year = "2001",
    volume = "40",
    number = "19",
    pages = "3603-3605",
    issn = "1433-7851, 1521-3773",
    doi = "10.1002/1521-3773(20011001)40:19<3603::AID-ANIE3603>3.0.CO;2-5",
    keywords = "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",
    abstract = "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."
}