Intermolecular Interactions

Protein structure is stabilized by weak, non-covalent interactions

  • The typical stability for a folded protein is only about 20-60 kJ/mol

Stabilizing interactions:

  • Covalent and coordinate bonding
  • Hydrogen bonding
  • salt bridges (charge/charge)
  • vander Waals interactions (dipole/dipole;induced dipole/induced dipole)
  • Hydrophobic effect