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

Topics Community

Article

Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase.

The journal of physical chemistry. B - 24 Oct 2024

Kalmer Thomas L, Ancajas Christine Mae F, Cohen Cameron I, McDaniel Jade M, Oyedele Abiodun S, Thirman Hannah L, Walker Allison S

Abstract excerpt

Dihydrofolate reductase (DHFR), due to its universality and the depth with which it has been studied, is a model system in the study of protein dynamics. Myriad previous works have identified networks of residues in positions near to and remote from the active site that are involved in the dynamics. For example, specific mutations on the Met20 loop in Escherichia coli DHFR (N23PP/S148A) are known to disrupt...

Topics

Join the communities discussing this publication.

Allosteric Regulation
Escherichia coli
DHFR gene
Molecular Dynamics Simulation
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Tetrahydrofolate Dehydrogenase

Source

Open in PubMed Open full text

Identifiers

PMID: 39385339
DOI: 10.1021/acs.jpcb.4c04195
PMCID: PMC11514014

Genes

DHFR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase.PMID 39385339Read ↗

Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate ReductaseSemantic proximity Read ↗

Allosteric regulatory control in dihydrofolate reductase is revealed by dynamic asymmetry.Semantic proximity Read ↗

Computational methods for predicting sites of functionally important dynamics.Semantic proximity Read ↗

On the accuracy of inferring energetic coupling between distant sites in protein families from evolutionary imprints: illustrations using lattice model.Semantic proximity Read ↗

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

Divergent evolution of protein conformational dynamics in dihydrofolate reductase.Semantic proximity Read ↗

Preservation of protein dynamics in dihydrofolate reductase evolution.Semantic proximity Read ↗

DHFR Mutants Modulate Their Synchronized Dynamics with the Substrate by Shifting Hydrogen Bond Occupancies.Semantic proximity Read ↗

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

Dynamical network of residue-residue contacts reveals coupled allosteric effects in recognition, catalysis, and mutation.Semantic proximity Read ↗

Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.Semantic proximity Read ↗

Distal Regions Regulate Dihydrofolate Reductase-Ligand Interactions.Semantic proximity Read ↗

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