List of bonding in protein folding

covalent bond (disulfide bridges)

ionic bonds
hydrogen bonds
hydrophobic bonds
van der waals forces
1. covalent bond (disulfide bridges)
links amino acids in a protein chain by peptide bond
arise when 2 atoms are sharing electron
strongest chemical bond that contributing to proteins structure
2. Ionic bonds (salts bridges)

Formed as amino acids bearing opposite electrical charges are getting closer in
hydrophobic core of proteins.
Important to protein structure because they are potent electrostatic attractions that
can approach the strength of covalent bonds.

3. Hydrogen bonds (H-H)

Form when 2 atoms bearing partial negative charges share a partially positive
charged hydrogen.
Plays an important role in maintaining the 3D structure of protein.
Stronger than Van Der Waals forces but weaker than ionic and covalent bonds.

4. Hydrophobic bonds

a major force driving proper protein folding.

Forms an interior, hydrophobic protein core, where most hydrophobic sidechains can
closely associate and are sheilded from interactions with water.
Weakest bond.

5. Van Der Waals Forces

a transsient, weak electrical attraction of one atom for another.

Exist because every atom has an electron cloud that can fluctuate, yielding a
temporary electric dipole
Play important roles in protein- protein recognition when complementary shapes are
involved.
Weaker bond than covalent and hydrogen but stronger than hydrophobic bond.