For proteins, so-called additive schemes exist, which allow predicting the partial molar heat capacity of the denatured (unfolded) state for any protein based on the number of individual amino acids in that protein, which is crucial for stability research. In this master's thesis, I undertook the investigation of the additivity of the partial heat capacity of nucleotides in DNA and the development of an equation that would serve as an additive scheme for estimating the partial molar heat capacity of denatured (unfolded) states of arbitrary single-stranded DNA based on measuring the partial molar heat capacity of shorter model compounds (DNA oligonucleotides) using differential scanning calorimetry (DSC). I determined the contributions for individual nucleotides (A, T, C, G) and as such parameterized the equation for predicting the partial molar heat capacity. The predicted values roughly match the data, indicating that the parameters in the equation need improvement. Potential for improvement lies in considering the surroundings or nearest neighbors, which have a significant influence on the contribution of individual nucleotides to the partial molar heat capacity.
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