Ontology highlight
ABSTRACT:
SUBMITTER: Schledorn M
PROVIDER: S-EPMC4429654 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Schledorn Maarten M Meier Beat H BH Böckmann Anja A
Frontiers in molecular biosciences 20150428
Recently the 3D structure of the Osaka mutant form (E22Δ) of Amyloid-β1-40 has been determined. We here compare the NMR chemical-shift with the published shifts of a brain-seeded form of wild-type Aβ and suggest that the determined mutant fold is accessible to the wild-type protein as well, with small conformational adaptations which accommodate the E22 residue missing in the Osaka mutant. In addition, we illustrate how other mutants could also conform to this model. The stabilization of the N-t ...[more]