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-lived states to monitor protein unfolding by proton NMR.

Chemphyschem : a European journal of chemical physics and physical chemistry - 24 Oct 2011

Bornet Aurélien, Ahuja Puneet, Sarkar Riddhiman, Fernandes Laetitia, Hadji Sonia, Lee Shirley Y, Haririnia Aydin, Fushman David, Bodenhausen Geoffrey, Vasos Paul R

Abstract excerpt

The relaxation of long-lived states (LLS) corresponds to the slow return to statistical thermal equilibrium between symmetric and antisymmetric proton spin states. This process is remarkably sensitive to the presence of external spins and can be used to obtain information about partial unfolding of proteins. We detected the appearance of a destabilized conformer of ubiquitin when urea is added to the protein in...

Read the complete abstract on PubMed

Topics

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

Share to Hydrogen Bonding
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Stability

Share to Protein Unfolding

Share to Protons

Share to Ubiquitin

Source

Open in PubMed Open full text

Identifiers

PMID: 21882334
DOI: 10.1002/cphc.201100365
PMCID: PMC3368952

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

Long-lived states to monitor protein unfolding by proton NMR.PMID 21882334Read ↗

Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.Semantic proximity Read ↗

A hydrogen bond regulates slow motions in ubiquitin by modulating a β-turn flip.Semantic proximity Read ↗

Protein conformational dynamics studied by 15N and 1H R1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals.Semantic proximity Read ↗

Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences.Semantic proximity Read ↗

Detection of altered protein conformations in living cells.Semantic proximity Read ↗

DOTA-M8: An extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy.Semantic proximity Read ↗

Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.Semantic proximity Read ↗

Differences in dynamic structure of LC8 monomer, dimer, and dimer-peptide complexes.Semantic proximity Read ↗

Simultaneous measurement of 1HC/N-R2's for rapid acquisition of backbone and sidechain paramagnetic relaxation enhancements (PREs) in proteins.Semantic proximity Read ↗

Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein-Protein and Protein-Ligand Interactions.Semantic proximity Read ↗

Interactions Controlling the Slow Dynamic Conformational Motions of Ubiquitin.Semantic proximity Read ↗

Probing the folding transition state of ubiquitin mutants by temperature-jump-induced downhill unfolding.Semantic proximity Read ↗

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