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

Exploring the mechanism of DNA polymerases by analyzing the effect of mutations of active site acidic groups in Polymerase β.

Proteins - 1 Nov 2016

Matute Ricardo A, Yoon Hanwool, Warshel Arieh

Abstract excerpt

Elucidating the catalytic mechanism of DNA polymerase is crucial for a progress in the understanding of the control of replication fidelity. This work tries to advance the mechanistic understanding by analyzing the observed effect of mutations of the acidic groups in the active site of Polymerase β as well as the pH effect on the rate constant. The analysis involves both empirical valence bond (EVB) free energy...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Aspartic Acid
Share to DNA Polymerase beta

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

Share to Glutamic Acid

Share to Molecular Dynamics Simulation

Share to Protein Domains

Share to Protons

Share to Quantum Theory

Source

Open in PubMed Open full text

Identifiers

PMID: 27488241
DOI: 10.1002/prot.25106
PMCID: PMC5073053

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring the mechanism of DNA polymerases by analyzing the effect of mutations of active site acidic groups in Polymerase β.PMID 27488241Read ↗

Distal Mutations in the β-Clamp of DNA Polymerase III* Disrupt DNA Orientation and Affect Exonuclease Activity.Semantic proximity Read ↗

Computational Simulations of DNA Polymerases: Detailed Insights on Structure/Function/Mechanism from Native Proteins to Cancer Variants.Semantic proximity Read ↗

Optimal and variant metal-ion routes in DNA polymerase β's conformational pathways.Semantic proximity Read ↗

Unfavorable electrostatic and steric interactions in DNA polymerase β E295K mutant interfere with the enzyme's pathway.Semantic proximity Read ↗

Effects of the Y432S Cancer-Associated Variant on the Reaction Mechanism of Human DNA Polymerase κ.Semantic proximity Read ↗

Requirement for transient metal ions revealed through computational analysis for DNA polymerase going in reverse.Semantic proximity Read ↗

Highly organized but pliant active site of DNA polymerase beta: compensatory mechanisms in mutant enzymes revealed by dynamics simulations and energy analyses.Semantic proximity Read ↗

Identification of the acidic residues in the active site of DNA polymerase III.Semantic proximity Read ↗

Structural changes in the hydrophobic hinge region adversely affect the activity and fidelity of the I260Q mutator DNA polymerase β.Semantic proximity Read ↗

Simulating the effect of DNA polymerase mutations on transition-state energetics and fidelity: evaluating amino acid group contribution and allosteric coupling for ionized residues in human pol beta.Semantic proximity Read ↗

Revealing an Internal Stabilization Deficiency in the DNA Polymerase β K289M Cancer Variant through the Combined Use of Chemical Biology and X-ray Crystallography.Semantic proximity Read ↗

Hinge residue Ile260 of DNA polymerase beta is important for enzyme activity and fidelity.Semantic proximity Read ↗

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