Calorimetry Studies

CBI offers both differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC) protocols. A DSC thermogram of any macromolecule will give information about the thermal stability of that molecule. From a DSC experiment, the heat necessary to unfold a structured macromolecule is measured and recorded as a function of increasing temperature. Molecules which posess multiple domain often display multiple transitions, and we routinely examine the unfolding pathways of native and recombinant proteins, synthetic DNAs, synthetic peptides, etc.

ITC affords simultaneous determination of the thermodynamic parameters relevant to ligand binding to macromolecules, including Ka, the association constant, and N, the stoichiometry between ligand and macromolecule, as well as the enthalpic (delta H) and entropic (delta S) contributions to the free energy of association (delta G). We have successfully used ITC to examine binding between proteins, between peptides and proteins, between peptides or proteins and saccharides, between antibodies and antigens, and between peptides and low molecular weight solutes.

As with all calorimetry protocols, the amounts of materials required are higher than for other analytical techniques. Please inquire for details of these experiments.

Calorimetry Prices

Both DSC and ITC are $280 per run.

Prices subject to change without notice

Please call 800-735-9224 or e-mail for additional information.