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

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

Solid state nuclear magnetic resonance - 1 Oct 2017

Gauto Diego F, Hessel Audrey, Rovó Petra, Kurauskas Vilius, Linser Rasmus, Schanda Paul

Abstract excerpt

Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45-60kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Mutation

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Conformation

Share to Ubiquitin

Source

Open in PubMed Open full text

Identifiers

PMID: 28438365
DOI: 10.1016/j.ssnmr.2017.04.002
PMCID: PMC5531261

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

Protein conformational dynamics studied by 15N and 1H R1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals.PMID 28438365Read ↗

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

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function.Semantic proximity Read ↗

Visualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switch.Semantic proximity Read ↗

Long-lived states to monitor protein unfolding by proton NMR.Semantic proximity Read ↗

Rapid acquisition of multidimensional solid-state NMR spectra of proteins facilitated by covalently bound paramagnetic tags.Semantic proximity Read ↗

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

A compare-and-contrast NMR dynamics study of two related RRMs: U1A and SNF.Semantic proximity Read ↗

NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin.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 ↗

Characterizing RNA Excited States Using NMR Relaxation Dispersion.Semantic proximity Read ↗

Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core.Semantic proximity Read ↗

Activation Dynamics of Ubiquitin Specific Protease 7Semantic proximity Read ↗

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