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Protein stability is crucial in various in vitro protein studies and is a major prerequisite in functional studies involving native and recombinant proteins. Proteins are in a state of steady flux and have particularly defined half-lives, being constantly synthesized and degraded inside the cell. Their basic and functional properties can be easily influenced by unfavorable conditions, such as sudden changes in temperature or pH, presence of proteases, and mechanical disturbance.

Differential scanning calorimetry (DSC) is a strategy used to characterize protein stability by measuring the amount of heat required to denature a biomolecule. Protein stability is also a major concern in 2D and 3D crystallization, and parameters can be estimated by inducing an unfolding reaction using chemical denaturants. Various techniques, including CD spectroscopy, can be used to monitor chemical-induced denaturation.

Stabilizing forces, such as non-covalent interactions, act together to maintain a protein's proper folding and stability under physiological conditions. Protein structure portrays the particular shape that a protein takes on, and chemical bonds, like hydrogen bonds, act like glue to hold these structures together. A protein's essential amino acid sequence is a huge figure in deciding which of these chemical bonds can form, and where.