Solid state NMR reveals a pH-dependent antiparallel β-sheet registry in fibrils formed by a β-amyloid peptide

Journal of Molecular Biology

Volumn 335, Issue 1, 2004, Pages 247-260

  Petkova, A T ^a   Buntkowsky, G ^b   Dyda, F ^a   Leapman, R D ^c   Yau, W M ^a   Tycko, R ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Alzheimer's disease; Amyloid fibrils; Antiparallel sheets; Hydrogen bond registry; Solid state NMR

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[11-25]; AMYLOID BETA PROTEIN[16-22]; HYDROGEN; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; FIBER; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR PROBE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SOLID STATE; SUPRAMOLECULAR CHEMISTRY; X RAY DIFFRACTION;

EID: 0344255649     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.044     Document Type: Article

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