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

Correlated motion and the effect of distal mutations in dihydrofolate reductase.

Proceedings of the National Academy of Sciences of the United States of America - 10 Jun 2003

Rod Thomas H, Radkiewicz Jennifer L, Brooks Charles L

Abstract excerpt

Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate to tetrahydrofolate. The catalytic rate in this system has been found to be significantly affected by mutations far from the site of chemical activity in the enzyme [Rajagopalan, P. T. R, Lutz, S., and Benkovic, S. J. (2002)...

Read the complete abstract on PubMed

Topics

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

Share to Computer Simulation
Share to Hydrogen Bonding
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Motion

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Tetrahydrofolate Dehydrogenase

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 12756296
DOI: 10.1073/pnas.1230801100
PMCID: PMC165816

Genes

DHFR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12756296-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Correlated motion and the effect of distal mutations in dihydrofolate reductase.PMID 12756296Read ↗

Effect of Asp122 Mutation on the Hydride Transfer in E. coli DHFR Demonstrates the Goldilocks of Enzyme Flexibility.Semantic proximity Read ↗

Simulations of remote mutants of dihydrofolate reductase reveal the nature of a network of residues coupled to hydride transfer.Semantic proximity Read ↗

Effect of mutation on enzyme motion in dihydrofolate reductase.Semantic proximity Read ↗

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

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

The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase.Semantic proximity Read ↗

Effects of a distal mutation on active site chemistry.Semantic proximity Read ↗

A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.Semantic proximity Read ↗

Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.Semantic proximity Read ↗

The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.Semantic proximity Read ↗

The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies.Semantic proximity Read ↗

Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase.Semantic proximity Read ↗

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