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Differential Scanning Calorimetry of Proteins

1995; Springer Nature; Linguagem: Inglês

10.1007/978-1-4899-1727-0_6

2542-8810

José M. Sánchez‐Ruiz,

thermodynamics and calorimetric analyses

Differential scanning calorimetry (DSC) is a powerful technique to characterize temperature-induced conformational changes in proteins and other biological macromolecules. In fact, DSC studies on protein thermal denaturation have played a central role in the development of current views about the factors that determine protein stability. Reviews on the various aspects of this technique are available in the literature (see, for instance, Privalov, 1979, 1982, 1989; Mateo, 1984; Sturtevant, 1987; Sanchez-Ruiz and Mateo, 1987; Freire et al., 1990) and, consequently, this chapter will mainly focus on recent developments in the field. The relevant features of the DSC experiment and the preliminary data analysis will be outlined in this section, and the well-known equilibrium thermodynamics procedures for the analysis of the DSC profiles will be briefly summarized in Section 2.