Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Polymorphic triple beta-sheet structures contribute to amide hydrogen/deuterium (H/D) exchange protection in the Alzheimer amyloid beta42 peptide.

The Journal of biological chemistry - 30 Sept 2011

Ma Buyong, Nussinov Ruth

Abstract excerpt

Characterization of the polymorphic structural range of Aβ oligomers is important to the understanding of the mechanisms of toxicity. Yet for highly polymorphic ensembles, experimental structural elucidation is difficult. Here, we use a combination of NMR solvent protection experiments and computational structural screening to identify major species in the amyloid conformational ensemble. We examined the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alzheimer Disease
Share to Amyloid
Share to Amyloid beta-Peptides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Deuterium Exchange Measurement

Share to Models, Chemical

Share to Mutation

Share to Peptide Fragments

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 21832091
DOI: 10.1074/jbc.M111.241141
PMCID: PMC3190809

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Polymorphic triple beta-sheet structures contribute to amide hydrogen/deuterium (H/D) exchange protection in the Alzheimer amyloid beta42 peptide.PMID 21832091Read ↗

Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.Semantic proximity Read ↗

Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformation.Semantic proximity Read ↗

Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solution.Semantic proximity Read ↗

Structural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides.Semantic proximity Read ↗

Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Semantic proximity Read ↗

Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.Semantic proximity Read ↗

Conformational Ensembles of the Wild-Type and S8C Aβ1-42 Dimers.Semantic proximity Read ↗

Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Semantic proximity Read ↗

Impact of A2T and D23N Mutations on Tetrameric Aβ42 Barrel within a Dipalmitoylphosphatidylcholine Lipid Bilayer Membrane by Replica Exchange Molecular Dynamics.Semantic proximity Read ↗

Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.Semantic proximity Read ↗

Effects of the Arctic (E22-->G) mutation on amyloid beta-protein folding: discrete molecular dynamics study.Semantic proximity Read ↗

Alzheimer's Protective Cross-Interaction between Wild-Type and A2T Variants Alters Aβ42 Dimer Structure.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.