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

Long-range correlated dynamics in intrinsically disordered proteins.

Journal of the American Chemical Society - 19 Nov 2014

Parigi Giacomo, Rezaei-Ghaleh Nasrollah, Giachetti Andrea, Becker Stefan, Fernandez Claudio, Blackledge Martin, Griesinger Christian, Zweckstetter Markus, Luchinat Claudio

Abstract excerpt

Intrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP α-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Synuclein
Share to Chemical Phenomena

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Intrinsically Disordered Proteins

Share to Models, Molecular

Share to Protein Conformation

Share to Protons

Share to Temperature

Source

Identifiers

PMID: 25331250
DOI: 10.1021/ja506820r

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Long-range correlated dynamics in intrinsically disordered proteins.PMID 25331250Read ↗

The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than millisecondsSemantic proximity Read ↗

Ensemble docking for intrinsically disordered proteinsSemantic proximity Read ↗

Precise Generation of Conformational Ensembles for Intrinsically Disordered Proteins via Fine-tuned Diffusion ModelsSemantic proximity Read ↗

Precise Generation of Conformational Ensembles for Intrinsically Disordered Proteins via Fine-tuned Diffusion ModelsSemantic proximity Read ↗

Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion.Semantic proximity Read ↗

Hierarchical Ensembles of Intrinsically Disordered Proteins at Atomic Resolution in Molecular Dynamics SimulationsSemantic proximity Read ↗

Glassy dynamics in mutant huntingtin proteins.Semantic proximity Read ↗

Intrinsic motions in the N-terminal domain of an ionotropic glutamate receptor detected by fluorescence correlation spectroscopy.Semantic proximity Read ↗

Exploring the essential collective dynamics of interacting proteins: application to prion protein dimers.Semantic proximity Read ↗

Resolving Local and Global Conformational Heterogeneity of the Human Intrinsically Disordered ProteomeSemantic proximity Read ↗

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

The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.Semantic proximity Read ↗

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