This protocol can be applied to analyze the direct interaction between a soluble protein and a target ligand molecule using Isothermal Titration Calorimetry (ITC, Malvern). ITC allows the biophysical characterization of binding between label-free, non-immobilized and in-solution biomolecules by providing the stoichiometry of the interaction, the equilibrium binding constants and the thermodynamic parameters. ITC monitors heat changes (released and/or absorbed) caused by macromolecular interactions with no restrictions of buffer and molecular weight of the macromolecules.
Isothermal Titration Calorimetry : A Biophysical Method to Characterize the Interaction between Label-free Biomolecules in Solution / A.C. Saponaro. - In: BIO-PROTOCOL. - ISSN 2331-8325. - 18:15(2018 Aug 05), pp. e2957.1-e2957.11. [10.21769/BioProtoc.2957]
Isothermal Titration Calorimetry : A Biophysical Method to Characterize the Interaction between Label-free Biomolecules in Solution
A.C. Saponaro
Primo
2018
Abstract
This protocol can be applied to analyze the direct interaction between a soluble protein and a target ligand molecule using Isothermal Titration Calorimetry (ITC, Malvern). ITC allows the biophysical characterization of binding between label-free, non-immobilized and in-solution biomolecules by providing the stoichiometry of the interaction, the equilibrium binding constants and the thermodynamic parameters. ITC monitors heat changes (released and/or absorbed) caused by macromolecular interactions with no restrictions of buffer and molecular weight of the macromolecules.File | Dimensione | Formato | |
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