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

Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.

Scientific reports - 8 Sept 2015

Chong Song-Ho, Hong Jooyeon, Lim Sulgi, Cho Sunhee, Lee Jinkeong, Ham Sihyun

Abstract excerpt

β-2-microglobulin (β2m) self-aggregates to form amyloid fibril in renal patients taking long-term dialysis treatment. Despite the extensive structural and mutation studies carried out so far, the molecular details on the factors that dictate amyloidogenic potential of β2m remain elusive. Here we report molecular dynamics simulations followed by the solvation thermodynamic analyses on the wild-type β2m and D76N,...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidogenic Proteins
Share to beta 2-Microglobulin

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Molecular Dynamics Simulation

Share to Protein Conformation

Share to Protein Stability

Share to Solvents

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 26348154
DOI: 10.1038/srep13631
PMCID: PMC4562173

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.PMID 26348154Read ↗

Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.Semantic proximity Read ↗

The folding space of protein <i>β</i> 2-microglobulin is modulated by a single disulfide bridgeSemantic proximity Read ↗

D-strand perturbation and amyloid propensity in beta-2 microglobulin.Semantic proximity Read ↗

Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Semantic proximity Read ↗

DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form.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 ↗

Conformational Features of Aβ25-35 and Its Mutants Suggest Toxic Structural Determinants: Insights from REST2 Simulations.Semantic proximity Read ↗

A Self-Consistent Molecular Mechanism of β2-Microglobulin Aggregation.Semantic proximity Read ↗

The effects of an ideal beta-turn on beta-2 microglobulin fold stability.Semantic proximity Read ↗

Characterization of Salt-Induced Oligomerization of Human β2-Microglobulin at Low pH.Semantic proximity Read ↗

BenchIDPs: Evaluation of Conformational Preferences Molecular Mechanics and Solvent Interactions of IDPs across popular Force Fields and Water ModelsSemantic proximity Read ↗

Disease-relevant β2-microglobulin variants share a common amyloid foldSemantic proximity Read ↗

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