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Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
The deconvolution of differential scanning calorimetry unfolding transitions
1Chemistry Department, State University of New York - Cortland, United States.
Abstract:
This paper is a review of a process for deconvolution of unfolding thermal transitions measured by differential scanning calorimetry. The mathematical background is presented along with illustrations of how the unfolding data is processed to resolve the number of sequential transitions needed to describe an unfolding mechanism and to determine thermodynamic properties of the intermediate states. Examples of data obtained for a simple two-state unfolding of a G-quadruplex DNA structure derived from the basic human telomere sequence, (TTAGGG)4TT are used to present some of the basic issues in treating the DSC data. A more complex unfolding mechanism is also presented that requires deconvolution of a multistate transition, the unfolding of a related human telomere structure, (TTAGGG)12 TT. The intent of the discussion is to show the steps in deconvolution, and to present the data at each step to help clarify how the information is derived from the various mathematical manipulations.
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