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Abstract

Protein stability may be understood as the resistance of a protein against the denaturing action of physical or chemical factors (e.g., temperature, pH, addition of solutes etc.). Usually, various factors may induce quite different changes in the protein such as loss of activity, changes of spectral properties and other physical parameters or even cleavage of the polypeptide chain. To quantitate protein stability, the conformational stability is commonly used. Under physiological conditions the folded (native) and unfolded (denatured) states of a protein are in equilibrium. The Gibbs energy change (ΔG) for the equilibrium reaction taking place without cleavage of covalent bonds

$${\text{folded }}(N){\text{ }} \rightleftharpoons {\text{ unfolded }}({\text{D}})$$

is referred to as the conformational stability of a protein. Thus, protein stability is defined on the sound basis of thermodynamic quantities. Therefore, it is possible to compare proteins irrespective of their different biological activity, molecular mass etc. Moreover, related thermodynamic quantities such as enthalpy change (ΔH), entropy change (ΔS), and heat capacity change (ΔCp) at unfolding can be determined which allows to gain a deeper insight into the forces that stabilizethe unique three-dimensional structure.

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Pfeil, W. (1998). Introduction. In: Protein Stability and Folding. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-58760-3_1

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