Which calorimeters do you have ?

At this moment we have three Isothermal Titration Calorimeters - MS-ITC, VP-ITC and iTC200 which allowing to determine thermodynamic parameters of interaction in the wide range of association constants and enthalpies of binding. We have also Differential Scanning Calorimeter VP-DSC which allowing to study temperature denaturation of biomolecules (proteins, DNA/RNA, micelles) and their complexes in the range of temperature from 5 to 120 C.

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How many protein do you need for experiment?

The simple answer could be disappointing - from 0.1 to 1 mg both for ITC and DSC. But as almost for all methods it depends on a number of factors. In case of ITC experiments, first of all it depends on enthalpy and constant of binding. The higher enthalpy of binding - the lower concentration can be used for experiment. From the other hand to get good ITC curve and determine all thermodynamic parameters with high accuracy the ratio between concentration and binding constant should varied between 10 and 100.

Which interactions can be studied by ITC ?

Using ITC we can follow all reactions accompanied with heat exchange. Thus the wide class of biomolecular interactions could be studied by ITC including protein-protein, protein-DNA, protein-drugs, protein-ions, DNA-ions and so on. Contrary to other methods the is no size limitations or need for molecule labeling. Nevertheless, some entropy driven reactions proceed with very low heat exchange or even without heat exchange at all. Sometimes it is possible to bypass this limitation performing ITC experiment at different temperatures.

What is the range of constants can be determined by ITC ?

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