Abstract
In some cases, small globular domains can maintain their native three-dimensional structure when separated from the rest of the protein. But due to the small size of such domains and low heat effect accompanying their cooperative structure unfolding, this transition occurs in a very broad temperature range. It is shown that for such broad processes an accurate evaluation of the . parameters from the DSC data can be done only by a global curve-fitting analysis applied to the multiple DSC curves obtained under various solvent conditions.
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