How do hydrophobic amino acids and hydrophilic amino acids cause proteins to have a specific shape?

There are many different amino acids in amino acid chains. Some of these amino acids form alpha helices, while others form beta sheets, which are instances of secondary structure.

But amino acids are essentially divided into two categories: those that are attracted to water and those that are repelled by it. For example, if you mix a drop of cooking oil with water and observe what happens, you will notice that the oil is separated into tiny, fine particles that eventually condense back into the original drop. This is because the larger drop gives the amino acids less surface area to interact with the water.

The hydrophobic effect is the result of all the hydrophobic amino acids, which are like the tiny drops of oil above, wanting to escape the water and condense to the middle. Once this is accomplished, the interaction between the polar groups and hydrogen bonds stabilizes the overall three-dimensional structure of the protein both inside and outside, but the process is primarily driven by the internal condensation of all those hydrophobic amino acids.

Whereas hydrophilic amino acids are usually found on the protein's surface, interacting with water molecules, hydrophobic amino acids tend to group together in the interior of a protein, away from water. This arrangement affects the folding and three-dimensional structure of the protein, giving it its particular shape.