Sensitivity Analysis of DSC Measurements of Denaturation of a Protein Mixture

Matt Ryerkerk
Under the direction of Dr. Neil Wright, Mechanical Engineering

Quantifying the kinetics of denaturation of heated proteins can lead to insight into protein folding, for example. Differential scanning calorimetery (DSC) measures changes in enthalpy of a specimen as its temperature is changed. DSC is a popular method to study the kinetics of polymers and biological materials. Increasingly, researchers are using DSC to measure changes in the enthalpy of mixtures of proteins and in cells. The confidence region of the parameters reported in these studies maybe unclear, because numerous parameters are being estimated using a single enthalpy trace. The present study examines using DSC to denature rattail tendon, which is predominantly Type I collagen. Analyzing the resulting data provides values for the kinetic parameters, in particular those describing a first-order Arrhenius model, governing the reaction. Several different methods for determining the parameters have been presented in past studies. In this study, the sensitivity of the parameters to the variables of the reaction, including the method to determine the parameters, is investigated. The results can be used to as a starting point to study the reliability of parameters for DSC experiments involving the denaturation of multiple proteins.