Can we predict the protein stability by comparing heat change values obtained by ITC experiment ( ucal/sec value) by keeping all other parameters same ( concentration, no. of injections etc.) ?
No ITC is performed at constant temperature and cannot be used to compare stability of proteins: you can use it to compare stability of different complexes, for example same protein binding different ligands.
To measure protein stability you can use CD or Fluorimetry.
There is also DSC, Differential Scanning Calorimetry (which instrument is similar to ITC) and is used to study protein stability, you can refer to Malvern website for more info: https://www.malvern.com/en/products/technology/differential-scanning-calorimetry
This question has already be asked: https://www.researchgate.net/post/How_can_we_comapre_protein_stability_using_Isothermal_Titration_Calorimetry - what are you proposing to inject in your ITC experiments to perturb stability? For chemical denaturation, usually the concentrations of denaturant needed to perturb the stability (in the molar range) are so high that chemical denaturation is not compatible with an ITC setup
It depends on the type of stability you want to assess. As Domenico and Annemarie said, the structural stability must be determined by other techniques, since: ITC is performed at constant temperature, and injection of chemical denaturant at the required concentration would result in extremely large background heats.
However, if you are interested in stability in solution (e.g. kinetic stability aginst precipitation/aggregation/degradation...) or interested in comparing production batches in biopharmaceutical manufacturing or determining shelf-life of a given biological molecule, then you can use ITC or any other technique that provides information about: structure, binding, activity, function...
Therefore, performing ITC experiments at different times you will get binding affinity, binding enthalpy, and binding stoichiometry (or active fraction of reactant) as a function of time. Those binding parameters will inform you about the time course stability (e.g., maybe binding affinity decreases with time, or maybe the active fraction of protein decreases with time...).
Dear Vivek Prakash . See the following useful link: https://pubs.rsc.org/en/content/getauthorversionpdf/C5NP00094G
Kindly check the following very good link: https://www2.mrc-lmb.cam.ac.uk/groups/hmm/techniqs/ITC.html
Also check please the following very good RG link: Article Isothermal Titration Calorimetry
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