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

Free energy contributions to direct readout of a DNA sequence.

The Journal of biological chemistry - 16 Sept 2005

Ferreiro Diego U, Dellarole Mariano, Nadra Alejandro D, de Prat-Gay Gonzalo

Abstract excerpt

The energetic contributions of individual DNA-contacting side chains to specific DNA recognition in the human papillomavirus 16 E2C-DNA complex is small (less than 1.0 kcal mol(-1)), independent of the physical and chemical nature of the interaction, and is strictly additive. The sum of the individual contributions differs 1.0 kcal mol(-1) from the binding energy of the wild-type protein. This difference...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Crystallography, X-Ray
Share to Databases, Protein

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

Share to Hydrogen Bonding

Share to Nucleic Acid Conformation

Share to Oncogene Proteins, Viral

Share to Thermodynamics

Share to Viral Proteins

Source

Identifiers

PMID: 16000299
DOI: 10.1074/jbc.M505706200

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

Free energy contributions to direct readout of a DNA sequence.PMID 16000299Read ↗

Experimental snapshots of a protein-DNA binding landscape.Semantic proximity Read ↗

Predicting the effects of basepair mutations in DNA-protein complexes by thermodynamic integration.Semantic proximity Read ↗

Experimentally based contact energies decode interactions responsible for protein-DNA affinity and the role of molecular waters at the binding interface.Semantic proximity Read ↗

DNA sequence-specific recognition by a transcriptional regulator requires indirect readout of A-tracts.Semantic proximity Read ↗

Allostery through DNA drives phenotype switching.Semantic proximity Read ↗

Anatomy of specific interactions between lambda repressor and operator DNA.Semantic proximity Read ↗

Crystal structure of the E2 DNA-binding domain from human papillomavirus type 16: implications for its DNA binding-site selection mechanismSemantic proximity Read ↗

A Kinetic Analysis of DNA Ejection from Tailed Phages Revealing the Prerequisite Activation EnergySemantic 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 ↗

Dynamics of the Extended String-Like Interaction of TFIIE with the p62 Subunit of TFIIH.Semantic proximity Read ↗

Energy triplets for writing epigenetic marks: insights from QM/MM free-energy simulations of protein lysine methyltransferases.Semantic proximity Read ↗

Experimental assignment of the structure of the transition state for the association of barnase and barstar.Semantic proximity Read ↗

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