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. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.