ArticleMethods in enzymology2016
Measuring the Kinetics of Molecular Association by Isothermal Titration Calorimetry.
Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Balancing acceleration and turnover in [1 + 1] tetra-imine bis-calix[4]pyrrole reactor for Huisgen cycloadditions.Nature communications · 2026Article
- Utilizing a cell-free protein synthesis platform for the biosynthesis of a natural product, caffeine.Synthetic biology (Oxford, England) · 2023Article
- The feasibility of determining kinetic constants from isothermal titration calorimetry data.Biophysical journal · 2022Article
- Temperature-Controlled Electrospray Ionization: Recent Progress and Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Review
- Isothermal Titration Calorimetry.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Studying biomolecular folding and binding using temperature-jump mass spectrometry.Nature communications · 2020Article
- Slow molecular recognition by RNA.RNA (New York, N.Y.) · 2017Article
- Biophysical Analyses for Probing Glycan-Protein Interactions.Advances in experimental medicine and biologyReview
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The real-time power response inherent in an isothermal titration calorimetry (ITC) experiment provides an opportunity to directly analyze association kinetics, which, together with the conventional measurement of thermodynamic quantities, can provide an incredibly rich description of molecular binding in a single experiment. Here, we detail our application of this method, in which interactions occurring with relaxation times ranging from slightly below the instrument response time constant (12.5 s in this case) to as large as 600 s can be fully detailed in terms of both the thermodynamics and kinetics. In a binding titration scenario, in the most general case an injection can reveal an association rate constant (kon). Under more restrictive conditions, the instrument time constant-corrected power decay following each injection is simply an exponential decay described by a composite rate constant (kobs), from which both kon and the dissociation rate constant (koff) can be extracted. The data also support the viability of this exponential approach, for kon only, for a slightly larger set of conditions. Using a bimolecular RNA folding model and a protein-ligand interaction, we demonstrate and have internally validated this approach to experiment design, data processing, and error analysis. An updated guide to thermodynamic and kinetic regimes accessible by ITC is provided.
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Registered trials
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