Resumen

ROMERO-ROMERO, Sergio; FERNANDEZ-VELASCO, D. Alejandro  y  COSTAS, Miguel. Protein Thermodynamic Stability. Educ. quím [online]. 2018, vol.29, n.3, pp.3-17. ISSN 0187-893X.  https://doi.org/10.22201/fq.18708404e.2018.3.64699.

Proteins are able to perform a great variety of functions when they are in their native state. This state is in equilibrium with a large number of inactive conformations that collectively are called the denatured state. Using differential scanning calorimetry (DSC), it is possible to evaluate the protein thermodynamic stability, i.e. the change in Gibbs free energy (ΔG) between the native and the denatured state, as well as the stability curve (variation of ΔG with temperature). In this work, we describe the general principles of DSC, discuss how to obtain the stability curve, and provide examples of stability curves for different proteins with TIM barrel topology.

Palabras llave : Thermodynamic; Proteins; Stability; Calorimetry; TIM barrel.

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