ArticleAnalytical biochemistry2013
Modeling complex equilibria in isothermal titration calorimetry experiments: thermodynamic parameters estimation for a three-binding-site model.
Article in Analytical biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
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- Structural and biophysical insights into RomR, MglB, and MglC interactions involved in regulating cell polarity in Myxococcus xanthus.The Journal of biological chemistry · 2025Article
- Applications of Isothermal Titration Calorimetry in Studying Biomimetic Nanocarriers.Biomolecules · 2025Review
- In Vitro Evaluation of Amide-Linked Coumarin Scaffolds for the Inhibition of α‑Synuclein and Tau Aggregation.ACS omega · 2025Article
- Closed and open structures of the eukaryotic magnesium channel Mrs2 reveal the auto-ligand-gating regulation mechanism.Nature structural & molecular biology · 2025Article
- Ionic-Liquid-Modified Nanoparticles as Potential Mucus Modulators for Nasal Drug Delivery.ACS applied nano materials · 2024Article
- Protein Binding Leads to Reduced Stability and Solvated Disorder in the Polystyrene Nanoparticle Corona.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Selective Near-Infrared Blood Detection Driven by Ionic Liquid-Dye-Albumin Nanointeractions.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate.Frontiers in nutrition · 2023Article
- High-affinity binding at quadruplex-duplex junctions: rather the rule than the exception.Nucleic acids research · 2022Article
- The role of polymeric chains as a protective environment for improving the stability and efficiency of fluorogenic peptide substrates.Scientific reports · 2022Article
- The archaeal glutamate transporter homologue GltPh shows heterogeneous substrate binding.The Journal of general physiology · 2022Article
- Quantitative Analysis of the Interactions of Metal Complexes and Amphiphilic Systems: Calorimetric, Spectroscopic and Theoretical Aspects.Biomolecules · 2022Review
- Physical networks from entropy-driven non-covalent interactions.Nature communications · 2021Article
- Isothermal Titration Calorimetry.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Native mass spectrometry reveals the initial binding events of HIV-1 rev to RRE stem II RNA.Nature communications · 2020Article
- Article
- Isothermal titration calorimetry and surface plasmon resonance analysis using the dynamic approach.Biochemistry and biophysics reports · 2020Article
- Real time calorimetric characterisation of clay - drug complex dispersions and particles.International journal of pharmaceutics: X · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Isothermal titration calorimetry (ITC) is a powerful technique that can be used to estimate a complete set of thermodynamic parameters (e.g., K(eq) (or ΔG), ΔH, ΔS, and n) for a ligand-binding interaction described by a thermodynamic model. Thermodynamic models are constructed by combining equilibrium constant, mass balance, and charge balance equations for the system under study. Commercial ITC instruments are supplied with software that includes a number of simple interaction models, for example, one binding site, two binding sites, sequential sites, and n-independent binding sites. More complex models, for example, three or more binding sites, one site with multiple binding mechanisms, linked equilibria, or equilibria involving macromolecular conformational selection through ligand binding, need to be developed on a case-by-case basis by the ITC user. In this paper we provide an algorithm (and a link to our MATLAB program) for the nonlinear regression analysis of a multiple-binding-site model with up to four overlapping binding equilibria. Error analysis demonstrates that fitting ITC data for multiple parameters (e.g., up to nine parameters in the three-binding-site model) yields thermodynamic parameters with acceptable accuracy.
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