Denaturation: Difference between revisions

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Latest revision as of 16:57, 22 March 2025

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.

Process[edit]

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[edit]

Denaturation can be caused by heat, acid, base, salts, organic solvents, or by other means, such as cell lysis or shearing. The denaturation of the proteins of egg white by heat—as when boiling an egg—causes an irreversible change in the protein structure. Denaturation can also be caused by certain chemicals, such as alcohol and formaldehyde, which disrupt the hydrogen bonds and disulphide bonds that hold the protein in shape.

Effects[edit]

Denaturation is a process that involves the disruption of forces that stabilize the protein structure, it does not break peptide bonds. Thus, denaturation does not affect the primary structure of the protein. The denatured protein can exhibit a wide range of characteristics, from loss of solubility to aggregation.

See Also[edit]

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