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

Interactions Controlling the Slow Dynamic Conformational Motions of Ubiquitin.

Molecules (Basel, Switzerland) - 28 Aug 2017

Kitazawa Soichiro, Yagi-Utsumi Maho, Kato Koichi, Kitahara Ryo

Abstract excerpt

Rational mutation of proteins based on their structural and dynamic characteristics is a useful strategy for amplifying specific fluctuations in proteins. Here, we show the effects of mutation on the conformational fluctuations and thermodynamic stability of ubiquitin. In particular, we focus on the salt bridge between K11 and E34 and the hydrogen bond between I36 and Q41, which are predicted to control the...

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 Magnetic Resonance Spectroscopy
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Conformation

Share to Protein Stability

Share to Thermodynamics

Share to Ubiquitin

Source

Open in PubMed Open full text

Identifiers

PMID: 28846639
DOI: 10.3390/molecules22091414
PMCID: PMC6151440

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

Interactions Controlling the Slow Dynamic Conformational Motions of Ubiquitin.PMID 28846639Read ↗

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

Mutational and Environmental Effects on the Dynamic Conformational Distributions of Lys48-Linked Ubiquitin Chains.Semantic proximity Read ↗

Salt-dependent non-catalytic allostery of human USP14-regulated 26S proteasomeSemantic proximity Read ↗

Dynamic hotspots in the Uba7 UFD direct UbcH8 recognitionSemantic proximity Read ↗

Rotamer strain as a determinant of protein structural specificity.Semantic proximity Read ↗

Elimination of the C-cap in ubiquitin - structure, dynamics and thermodynamic consequences.Semantic proximity Read ↗

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

Context-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics.Semantic proximity Read ↗

Rearrangement of charge-charge interactions in variant ubiquitins as detected by double-mutant cycles and NMR.Semantic proximity Read ↗

High-Resolution Mapping of the Folding Transition State of a WW Domain.Semantic proximity Read ↗

Site-specific hydrogen exchange of proteins: insights into the structures of amyloidogenic intermediates.Semantic proximity Read ↗

Mapping increased flexibility and conformational divergence via N-terminal helix-to-coil transition in USP12 mutant Y49N: a comprehensive in-detail normal mode simulation study.Semantic proximity Read ↗

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