The hydrophobic effect in protein folding.

In this review of protein folding we consider the noncovalent interactions existing between atoms or molecules at the molecular level. The electrostatic, Van der Waals, hydrogen bonding, and hydrophobic interactions are described and their contribution to protein conformation is discussed. The growing interest in the hydrophobic effect arises from its importance in the protein folding process, and a semiempirical simulation of the free energy of solvation is proposed. In most proteins, the different forces we describe contribute to the stability of the protein conformation in a complex way. However, in the case of the apolipoproteins and cytochrome C551, the energetic contributions are easily distinguished. For this reason, these proteins are used to illustrate the importance of the different energy fields.