Stability of Protein Structure

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Proteins are complex molecules with complex three-dimensional structures that determine their specific roles within cells.
These structures are susceptible to disruption by various factors like changes in temperature, pH, or exposure to chemicals.
When a protein loses its native structure, it’s said to be denatured, making it non-functional.
This can lead to cellular malfunctions and potentially contribute to diseases.
Stability is the potential of a pattern to survive over time, and therefore is integral to our understanding of biological systems and their evolution processes.
Protein stability is the net balance of forces, which determine whether a protein will be in its native folded confirmation or a denatured state.
Compositional stability
This means that the protein molecules must have the same chemical makeup.
The chemical homogeneity of a sample can often be determined using mass spectrometry or an SDS–PAGE gel.
Compositional homogeneity is typically compromised by post-translational modifications, such as glycosylation and proteolysis, which can affect the primary structure of the protein molecules and generate compositional variability.
Conformational stability
A large class of proteins, referred to as intrinsically disordered proteins (IDPs), contain significant levels of conformational disorder and, in some cases, have no discernable three-dimensional structure at all.
It is estimated that 40% of all human proteins contain at least one disordered segment and 25% are completely disordered.