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

Thermodynamics of Fab-ssDNA interactions: contribution of heavy chain complementarity determining region 3.

Biochemistry - 2 Nov 1999

Komissarov A A, Deutscher S L

Abstract excerpt

The recombinant anti-ssDNA Fab, DNA-1, and 16 heavy chain complementarity determining region 3 (HCDR3) mutant variants were selected for thermodynamic characterization of ssDNA binding. The affinity of Fab to (dT)(15) under different temperatures and cation concentrations was measured by equilibrium fluorescence quenching titration. Changes in the standard Gibbs free binding energy (DeltaG degrees ), enthalpy...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Antinuclear
Share to DNA, Single-Stranded
Share to Immunoglobulin Fab Fragments

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

Share to Immunoglobulin Heavy Chains

Share to Immunoglobulin Variable Region

Share to In Vitro Techniques

Share to Static Electricity

Share to Thermodynamics

Source

Identifiers

PMID: 10545187
DOI: 10.1021/bi991347l

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 · 8 closest

Thermodynamics of Fab-ssDNA interactions: contribution of heavy chain complementarity determining region 3.PMID 10545187Read ↗

Crystal Structure of a Soluble APOBEC3G Variant Suggests ssDNA to Bind in a Channel that Extends between the Two Domains.Semantic proximity Read ↗

The use of Ni-nitrilotriacetic acid agarose for estimation of affinities of hexahistidine-tagged Fab to single-stranded DNA.Semantic proximity Read ↗

V gene sequences of lupus-derived human IgM anti-ssDNA antibody: implication for the importance of the location of DNA-binding amino acids.Semantic proximity Read ↗

Ensemble and single-molecule biophysical characterization of D17.4 DNA aptamer-IgE interactions.Semantic proximity Read ↗

Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein.Semantic proximity Read ↗

Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactionsSemantic proximity Read ↗

Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactions.Semantic proximity Read ↗

Insights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies.Semantic proximity Read ↗

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