Denaturation

Definition

Denaturation is the process by which a protein loses its native structure and function due to external stress, such as heat or chemicals. This structural change is often irreversible and affects the protein's biological activity.

5 Must Know Facts For Your Next Test

1. Denaturation disrupts hydrogen bonds, ionic interactions, and disulfide bridges within a protein.
2. Common causes of denaturation include high temperatures, extreme pH levels, and exposure to detergents or solvents.
3. Denatured proteins often lose their solubility in water and may precipitate out of solution.
4. The primary structure (amino acid sequence) of the protein remains unchanged during denaturation.
5. Enzymes are particularly sensitive to denaturation because their catalytic activity depends on their specific three-dimensional shape.

Review Questions

• What types of bonds are disrupted during the denaturation of a protein?
• How does denaturation affect the solubility of proteins?
• Why are enzymes especially affected by denaturation?

Related terms

Primary Structure:

The linear sequence of amino acids in a polypeptide chain.

Secondary Structure: The local folded structures that form within a polypeptide due to hydrogen bonding, such as alpha-helices and beta-sheets.

Tertiary Structure: The overall three-dimensional shape of a single polypeptide chain, stabilized by various interactions between side chains.