A native protein is a protein in its natural, functional, and properly folded form (the form found in living cells).
Structure of native protein
A native protein usually has its secondary, tertiary, and sometimes quaternary structure intact.
That’s what gives it its specific shape and biological activity.
Summary
| Term | Meaning |
|---|---|
| Primary structure | Sequence of amino acids |
| Secondary structure | α-helix or β-pleated sheet (H-bonds) |
| Tertiary structure | 3D folding → active shape |
| Native protein | Protein in its functional 3D (tertiary or quaternary) form |
Secondary Structure Proteins
- Meaning: Local folding of polypeptide chains into α-helix or β-pleated sheets (held by hydrogen bonds).
- Examples:
- Keratin → mostly α-helix (found in hair, nails, wool).
- Fibroin → mostly β-pleated sheet (found in silk).
Tertiary Structure Proteins
- Meaning: 3D folding of a single polypeptide chain → forms a globular protein.
- Forces involved: H-bonds, disulfide bridges, ionic bonds, hydrophobic interactions.
- Examples:
- Myoglobin → stores oxygen in muscles.
- Lysozyme → enzyme that breaks bacterial cell walls.
- Ribonuclease → enzyme for RNA breakdown.
Quaternary Structure Proteins
- Meaning: Association of two or more polypeptide chains (subunits) in a functional complex.
- Examples:
- Hemoglobin → 4 subunits (2 α + 2 β chains).
- Insulin → made of multiple polypeptide chains (A and B chains linked by disulfide bonds).
- DNA polymerase → multi-subunit enzyme.