Summary –,
Article –
Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, typically a biologically functional one. It is an essential process in molecular biology and biochemistry because the specific structure of a protein determines its function in living organisms.
Stages of Protein Folding
Protein folding is generally considered to take place in several stages:
- Primary Structure Formation: The sequence of amino acids in a polypeptide chain.
- Secondary Structure Formation: Localized folding into structures such as alpha-helices and beta-sheets stabilized by hydrogen bonds.
- Tertiary Structure Formation: The overall 3D folding of a single polypeptide chain into a functional shape.
- Quaternary Structure Formation: Assembly of multiple polypeptide chains into a functional protein complex.
Factors Influencing Protein Folding
- Hydrophobic interactions: Nonpolar amino acids tend to cluster away from water.
- Hydrogen bonding: Stabilizes secondary and tertiary structures.
- Van der Waals forces: Contribute to protein stability.
- Disulfide bridges: Covalent bonds forming cross-links between cysteine residues.
- Chaperones: Specialized proteins that assist proper folding and prevent misfolding.
Importance of Correct Protein Folding
Proper folding is crucial because misfolded proteins can lead to diseases such as Alzheimer’s, Parkinson’s, and Cystic fibrosis. Thus, cells employ quality control mechanisms to ensure correct folding and to degrade defective proteins.
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