Protein denaturation

Process of partial or total alteration of the native secondary, and/or tertiary, and/or quaternary structures of proteins or nucleic acids resulting in a loss of bioactivity.

Note 1: Modified from the definition given in ref.

Note 2: Denaturation can occur when proteins and nucleic acids are subjected to elevated temperature or to extremes of pH, or to nonphysiological concentrations of salt, organic solvents, urea, or other chemical agents.

Note 3: An enzyme loses its catalytic activity when it is denaturized.

Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Protein denaturation is also a consequence of cell death. Denatured proteins can exhibit a wide range of characteristics, from conformational change and loss of solubility to aggregation due to the exposure of hydrophobic groups.

Protein folding is key to whether a globular protein or a membrane protein can do its job correctly. It must be folded into the right shape to function. But hydrogen bonds, which play a big part in folding, are rather weak, and it doesn't take much heat, acidity, varying salt concentrations, or other stress to break some and form others, denaturing the protein. This is one reason why tight homeostasis is physiologically necessary in many life forms.

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