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

Thermodynamic characterization of binding Oxytricha nova single strand telomere DNA with the alpha protein N-terminal domain.

Journal of molecular biology - 23 Jun 2006

Buczek Pawel, Horvath Martin P

Abstract excerpt

The Oxytricha nova telemere binding protein alpha subunit binds single strand DNA and participates in a nucleoprotein complex that protects the very ends of chromosomes. To understand how the N-terminal, DNA binding domain of alpha interacts with DNA we measured the stoichiometry, enthalpy (DeltaH), entropy (DeltaS), and dissociation constant (K(D-DNA)) for binding telomere DNA fragments at different temperatures...

Read the complete abstract on PubMed

Topics

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

Share to DNA, Protozoan
Share to DNA, Single-Stranded
Share to Electrolytes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Entropy

Share to Lithium Chloride

Share to Protein Subunits

Share to Telomere

Share to Telomere-Binding Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16678852
DOI: 10.1016/j.jmb.2006.02.082
PMCID: PMC2953474

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Thermodynamic characterization of binding Oxytricha nova single strand telomere DNA with the alpha protein N-terminal domain.PMID 16678852Read ↗

Solution conformations and interactions of alpha and beta subunits of the Oxytricha nova telomere binding protein: investigation by Raman spectroscopy.Semantic proximity Read ↗

Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein.Semantic proximity Read ↗

Biophysical analysis of Thermus aquaticus single-stranded DNA binding protein.Semantic proximity Read ↗

Structural and thermodynamic signatures of DNA recognition by Mycobacterium tuberculosis DnaA.Semantic proximity Read ↗

Identification of thermodynamically relevant interactions between EF-Tu and backbone elements of tRNA.Semantic proximity Read ↗

The quorum sensing transcriptional regulator TraR has separate binding sites for DNA and the anti-activator.Semantic proximity Read ↗

Impact of C-terminal domains of paralogous single-stranded DNA binding proteins from Streptomyces coelicolor on their biophysical properties and biological functions.Semantic proximity Read ↗

The carboxyl terminal of the archaeal nuclease NurA is involved in the interaction with single-stranded DNA-binding protein and dimer formation.Semantic proximity Read ↗

Monomer-tetramer equilibrium of the Escherichia coli ssb-1 mutant single strand binding protein.Semantic proximity Read ↗

Quaternary interactions and supercoiling modulate the cooperative DNA binding of AGT.Semantic proximity Read ↗

Thermodynamic characterization of the interaction between the human Y-box binding protein YB-1 and nucleic acids.Semantic proximity Read ↗

Two distinct DNA sequences recognized by transcription factors represent enthalpy and entropy optimaSemantic proximity Read ↗

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