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

Relaxation and single site multiple mutations to identify and control allosteric networks.

Methods (San Diego, Calif.) - 1 Aug 2023

Lee Eunjeong, Redzic Jasmina S, Zohar Eisenmesser Elan

Abstract excerpt

Advances in Nuclear Magnetic Resonance (NMR) spectroscopy have allowed for the identification and characterization of movements in enzymes over the last 20 years that has also revealed the complexities of allosteric coupling. For example, many of the inherent movements of enzymes, and proteins in general, have been shown to be highly localized but nonetheless still coupled over long distances. Such partial...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Catalytic Domain
Share to Magnetic Resonance Spectroscopy

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

Share to Mutagenesis

Share to Mutation

Share to Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 37302521
DOI: 10.1016/j.ymeth.2023.06.002
PMCID: PMC11066977

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Relaxation and single site multiple mutations to identify and control allosteric networks.PMID 37302521Read ↗

Networks of Dynamic Allostery Regulate Enzyme Function.Semantic proximity Read ↗

Rational coupled dynamics network manipulation rescues disease-relevant mutant cystic fibrosis transmembrane conductance regulatorSemantic proximity Read ↗

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variants.Semantic proximity Read ↗

Full and Partial Agonism of a Designed Enzyme Switch.Semantic proximity Read ↗

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variantsSemantic proximity Read ↗

50 years of allosteric interactions: the twists and turns of the models.Semantic proximity Read ↗

The origin of allosteric functional modulation: multiple pre-existing pathways.Semantic proximity Read ↗

Synergy of Mutation-Induced Effects in Human Vitamin K Epoxide Reductase: Perspectives and Challenges for Allo-Network Modulator Design.Semantic proximity Read ↗

What Mutagenesis Can and Cannot Reveal About Allostery.Semantic proximity Read ↗

Functional tunability from a distance: Rheostat positions influence allosteric coupling between two distant binding sitesSemantic proximity Read ↗

Structurally distributed surface sites tune allosteric regulation.Semantic proximity Read ↗

Evolutionary Adaptations in Biliverdin Reductase B: Insights into Coenzyme Dynamics and Catalytic Efficiency.Semantic proximity Read ↗

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