title: Dynamics of amyloid β fibrils revealed by solid-state NMR.
abstract: We have investigated the site-specific backbone dynamics of mature amyloid β (Aβ) fibrils using solid-state NMR spectroscopy. Overall, the known β-sheet segments and the turn linking these two β-strands exhibit high order parameters between 0.8 and 0.95, suggesting low conformational flexibility. The first approximately eight N-terminal and the last C-terminal residues exhibit lower order parameters between ∼0.4 and 0.8. Interestingly, the order parameters increase again for the first two residues, Asp(1) and Ala(2), suggesting that the N terminus could carry some structural importance.
authors: Institute of Medical Physics and Biophysics, University of Leipzig, D-04107 Leipzig, Germany.
authors: Holger A
authors: HA
authors: Scheidt
authors: Isabel
authors: I
authors: Morgado
authors: Sven
authors: S
authors: Rothemund
authors: Daniel
authors: D
authors: Huster
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
chemical_list: C545487:APP protein, human; D000682:Amyloid; D016564:Amyloid beta-Protein Precursor