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Stability of Proteins- Bonds involved

protein structure
Protein Structure : Bonds involved
  • Secondary structure; α and β helices are stabilised by H bond.
  • Tertiary structure is stabilised by di sulphide bond which is a covalent bond.
  • 3D confirmation of protein is maintained by non covalent interactions like electrostatic forces, hydrogen bonds, hydrophobic forces) and covalent interactions (di-sulphide bonds) apart from the peptide bond between individual amino acids.
  • Hydrophobic forces or bonding is the major non covalent interaction that determines protein structure, folding and stability.
  • Di-sulphide bond between cys residues is the major covalent interaction that stabilizes the 3D native protein.
  • Di-sulphide bonds are formed only in oxidising environment of ER and that is why secretory and membrane proteins have extensive di-sulphide bonds.
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