Introduction to the principles of isothermal titration calorimetry & MicroCal's ITC microcalorimeter. View the Malvern Panalytical Range of ITC solutions. www.malvernpanalytial.com/en/p...
Thank you, if you want more information on the theory and practice, read this white paper - www.malvern.com/en/support/resource-center/Whitepapers/WP150318ITCTheoryAndPractice.html
Thank you, we recently uploaded a new range a video focusing on DSC - ru-vid.com/group/PL2wIBTZfZRje-lNJtKUUaDm0KKAeMott-. You can also find the What is DSC in this playlist.
If enzymes are reusable, why would the ligand ever be saturated after the reaction equals equilibrium? Wouldn't the new product be relased and the previously-used enzymes would be available again?
Hello Angelo, The ITC can be run over a range of temperatures between 25 and 70 C. The experiments can be done at 37C and the most common temperature is 25 C for typical binding experiments.
Madre - thanks for your question and comment. Isothermal Titration Calorimetry (ITC) is a biophysical assay for measuring the binding affinity between two interacting molecules. Binding interactions include protein-drug, protein-protein, antibody-antigen, DNA-drug, DNA-protein, and all possible combinations. ITC is label-free, and can be used with any biomolecule in solution. Along with binding affinity, ITC is a direct measurement of the change in enthalpy (DH) due to binding, and one can get other thermodynamic parameters from an ITC experiment.
They are different. Isothermal Calorimetry is used to measure reactions at a single temperature e.g. dissolving of a compound in a solvent at 25 C or a decomposition process. Isothermal titration calorimetry measures the heat associated with the heat of binding of molecules in solution at increasing concentration ratios of molecule ‘x’ over molecule ‘Y’. Hope that helps.
We used the term ‘affinity’ in a generic way to describe how tightly molecules interact. It can be described quantitatively as an association constant (KA) or a dissociation constant (KD). As you say they, they have a reciprocal relationship. We find that many biochemists like to use the dissociation constant, KD, to describe the affinity because it has units of concentration and can be related to amount of sample they are using in their experiments. Thank you so much for reaching out and I hope that clarifies the situation.
