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

Effect of Alzheimer's Disease Causative and Protective Mutations on the Hydration Environment of Amyloid-β.

The journal of physical chemistry. B - 26 Mar 2020

Aggarwal Leena, Biswas Parbati

Abstract excerpt

This study investigates the local structure and dynamics of hydration water around the intrinsically disordered protein amyloid-β (Aβ) and its Alzheimer's disease causative N-terminus mutants, i.e., A2V, Taiwan (D7H), Tottori (D7N), and English (H6R), and the protective A2T mutant via atomistic MD simulations. The effect of mutations on the hydration environment around different domains of this protein is...

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 beta-Peptides
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Peptide Fragments

Source

Identifiers

PMID: 32130011
DOI: 10.1021/acs.jpcb.9b10425

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of Alzheimer's Disease Causative and Protective Mutations on the Hydration Environment of Amyloid-β.PMID 32130011Read ↗

Hydration Thermodynamics of the N-Terminal FAD Mutants of Amyloid-β.Semantic proximity Read ↗

Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42.Semantic proximity Read ↗

Effect of Taiwan mutation (D7H) on structures of amyloid-β peptides: replica exchange molecular dynamics study.Semantic proximity Read ↗

Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.Semantic proximity Read ↗

Stability of Osaka Mutant and Wild-Type Fibril Models.Semantic proximity Read ↗

Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.Semantic proximity Read ↗

Differentially heterogeneous hydration environment of the familial mutants of α-synuclein.Semantic proximity Read ↗

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

Effect of the Tottori familial disease mutation (D7N) on the monomers and dimers of Aβ40 and Aβ42.Semantic proximity Read ↗

Changes to the structure and dynamics in mutations of Aβ(21-30) caused by ions in solution.Semantic proximity Read ↗

Molecular Mechanism of Zinc-Dependent Oligomerization of Alzheimer's Amyloid-β with Taiwan (D7H) Mutation.Semantic proximity Read ↗

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