Isothermal Titration Calorimetry to Determine Apparent Dissociation Constants (K d) and Stoichiometry of Interaction (n) of C-di-GMP Binding Proteins.

Abstract

Isothermal titration calorimetry (ITC) is a commonly used biophysical technique that enables the quantitative characterization of intermolecular interactions in solution. Based on enthalpy changes (ΔH) upon titration of the binding partner (e.g., a small-molecule ligand such as c-di-GMP) to the molecule of interest (e.g., a receptor protein), the resulting… (More)
DOI: 10.1007/978-1-4939-7240-1_30

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@article{Matsuyama2017IsothermalTC, title={Isothermal Titration Calorimetry to Determine Apparent Dissociation Constants (K d) and Stoichiometry of Interaction (n) of C-di-GMP Binding Proteins.}, author={Bruno Y Matsuyama and Petya Violinova Krasteva and Marcos V. A. S. Navarro}, journal={Methods in molecular biology}, year={2017}, volume={1657}, pages={403-416} }