Native structure

Definition

The native structure of a protein is its functional three-dimensional form, maintained under physiological conditions. It is essential for the protein's biological activity.

5 Must Know Facts For Your Next Test

1. The native structure is stabilized by non-covalent interactions such as hydrogen bonds, ionic bonds, and hydrophobic interactions.
2. Denaturation disrupts the native structure, leading to loss of function.
3. Chaperone proteins assist in the correct folding of proteins into their native structures.
4. X-ray crystallography and NMR spectroscopy are techniques used to determine the native structure of proteins.
5. Mutations can alter amino acid sequences and potentially disrupt the native structure.

Review Questions

• What types of bonds stabilize a protein’s native structure?
• How does denaturation affect a protein's native structure?
• What role do chaperone proteins play in maintaining the native structure?

Related terms

Denaturation: The process by which a protein loses its native structure and function due to external stress or compounds.

Chaperone Proteins: Proteins that assist in the proper folding of other proteins to ensure they achieve their functional native structures.

X-ray Crystallography: A technique used to determine the atomic and molecular structure of a crystal, revealing the arrangement of atoms within a protein in its native state.