Dynamics of amyloid ? fibrils revealed by solid-state NMR.

ABSTRACT: We have investigated the site-specific backbone dynamics of mature amyloid ? (A?) fibrils using solid-state NMR spectroscopy. Overall, the known ?-sheet segments and the turn linking these two ?-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.

SUBMITTER: Scheidt HA 

PROVIDER: S-EPMC3265881 | biostudies-other | 2012 Jan

REPOSITORIES: biostudies-other