Final answer:
Protein folding is driven by ionic bonding, hydrogen bonding, disulfide linkages, and dispersion forces. Amino acids with charged, polar, or hydrophobic R groups are involved in each type of interaction.
Step-by-step explanation:
Protein folding is driven by four major types of attractive interactions: ionic bonding, hydrogen bonding, disulfide linkages, and dispersion forces.
The types of amino acids involved in each type of interaction are:
- Ionic bonding: Involves amino acids with charged R groups, such as lysine, arginine, and glutamate.
- Hydrogen bonding: Involves amino acids with polar R groups, such as serine, threonine, and asparagine.
- Disulfide linkages: Involves the amino acid cysteine, which can form covalent bonds with another cysteine residue.
- Dispersion forces: Involves interactions between hydrophobic amino acids, such as leucine, isoleucine, and valine.