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

Detection of Mutation-Induced Conformational Changes in an Intrinsically Disordered Protein by Double Quantum Coherence Electron Spin Resonance Methodology.

Journal of the American Chemical Society - 21 Jan 2026

Sinha Roy Aritro, Tsay Karen, Borbat Peter P, Destefano Audra, Han Songi, Srivastava Madhur, Freed Jack H

Abstract excerpt

Intrinsically disordered proteins (IDPs) underlie essential cellular functions and drive neurodegenerative diseases through mutation-induced structural changes, yet their conformational heterogeneity often evades crystallography and cryo-EM. Electron spin resonance (ESR) pulsed dipolar spectroscopy (PDS), which determines distance distributions between a pair of spin-labeled residues in a protein, can provide...

Read the complete abstract on PubMed

Topics

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

Share to Electron Spin Resonance Spectroscopy
Share to Intrinsically Disordered Proteins

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

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Quantum Theory

Share to Spin Labels

Share to tau Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 41493397
DOI: 10.1021/jacs.5c16298
PMCID: PMC13560464

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 18 Oct 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

Detection of Mutation-Induced Conformational Changes in an Intrinsically Disordered Protein by Double Quantum Coherence Electron Spin Resonance Methodology.PMID 41493397Read ↗

The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3.Semantic proximity Read ↗

Copper-based pulsed dipolar ESR spectroscopy as a probe of protein conformation linked to disease states.Semantic proximity Read ↗

Integrative determination of the atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington’s diseaseSemantic proximity Read ↗

Nanomolar Pulse Dipolar EPR Spectroscopy in Proteins; the Copper(II)-Copper(II) and Nitroxide-Nitroxide CasesSemantic proximity Read ↗

Integrative determination of atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington disease.Semantic proximity Read ↗

Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3.Semantic proximity Read ↗

Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study.Semantic proximity Read ↗

High-Resolution NMR H/D Exchange of Human Superoxide Dismutase Inclusion Bodies Reveals Significant Native Features Despite Structural Heterogeneity.Semantic proximity Read ↗

Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangementSemantic proximity Read ↗

Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy.Semantic proximity Read ↗

Investigation of alpha-synuclein fibril structure by site-directed spin labeling.Semantic proximity Read ↗

Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.Semantic proximity Read ↗

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