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The following are the four forces acting on the amino acids placed in water:  

1. Van der Waals forces: The natural stickiness of every single atom, resulting due to the movement of its electron cloud.  

2. Electrostatic charge: The ions of a side chain, which have either minus or plus charge.  

3. S-S bonds: Many sulfur-containing amino acids like cysteine situated in the distinct parts of the protein chain, associated with each other, forming a covalent bond, which connects together the two distinct parts of a protein molecule.  

4. Hydrogen bonds: As the oxygen of the water molecule is strong, it pulls the electron cloud away from its two hydrogens, making its hydrogen somewhat positive and thus possessing the tendency to associate with the negative poles on the adjacent molecules.  

Hydrophobic is defined as the tendency to repel or fail to mix with water. While hydrophilic is defined as possessing the tendency to mix with or dissolve in water.  

Hydrophilic amino acids are water-loving, while hydrophobic amino acids are water-hating. Hydrophilic amino acids will react in a manner, which is contrasting from their response to water. When positioned in oil, they will be more fascinated with each other in comparison to the surrounding molecules. The non-polar hydrophobic amino acids will not be herded in combination by the oil, as they were by water, so they will get dissolve efficiently.