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

Fitting two- and three-site binding models to isothermal titration calorimetric data.

Methods (San Diego, Calif.) - 1 Apr 2015

Brautigam Chad A

Abstract excerpt

As isothermal titration calorimetry (ITC) gains popularity for the characterization of enthalpies and equilibrium association constants of simple 1:1 biomolecular interactions, its use for more complex systems is growing. The method is increasingly used to study interactions in which a single bin...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Binding Sites
Share to Colorimetry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lactoferrin

Share to Models, Molecular

Share to Mutation

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 25484338
DOI: 10.1016/j.ymeth.2014.11.018
PMCID: PMC4591754

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25484338-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 9 closest

Fitting two- and three-site binding models to isothermal titration calorimetric data.PMID 25484338Read ↗

Label-Free Determination of the Dissociation Constant of Small Molecule-Aptamer Interaction by Isothermal Titration Calorimetry.Semantic proximity Read ↗

TitrationAnalysis: a tool for high throughput binding kinetics data analysis for multiple label-free platformsSemantic proximity Read ↗

Profiling the Interaction between Human Serum Albumin and Clinically Relevant HIV Reverse Transcriptase InhibitorsSemantic proximity Read ↗

Thermodynamics of Ras/effector and Cdc42/effector interactions probed by isothermal titration calorimetry.Semantic proximity Read ↗

A new general method for simultaneous fitting of temperature and concentration dependence of reaction rates yields kinetic and thermodynamic parameters for HIV reverse transcriptase specificity.Semantic proximity Read ↗

Thermodynamics and folding pathway of tetraloop receptor-mediated RNA helical packing.Semantic proximity Read ↗

Refinement of noncalorimetric determination of the change in heat capacity, DeltaC(p), of protein unfolding and validation across a wide temperature range.Semantic proximity Read ↗

The effectiveness of three multi-component binding models in describing the binary competitive equilibrium adsorption of two cytochrome b(5) mutants.Semantic proximity Read ↗

On the fitting of binding data when receptor dimerization is suspected.Semantic proximity Read ↗

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