Denaturation (biochemistry)

Denaturation (biochemistry)

Denaturation is a process in biochemistry where 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.

Process

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.

Causes

Denaturation can be caused by heat, pH changes, or by chemicals. When proteins are subjected to high temperatures, the heat energy that's transferred to the protein can break the weak bonds that hold the protein in its secondary and tertiary structure.

Effects

Denatured proteins can often still function, but they are less efficient. The process of denaturation can also cause proteins to stick together, or aggregate. This can lead to a variety of diseases, such as Alzheimer's disease and Parkinson's disease.

See also

• Protein folding
• Protein structure
• Protein biosynthesis
• Protein targeting

References

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