Generally, globular proteins are made of egg albumin, hemoglobin, myoglobin, insulin, serum globulins in blood, and many enzymes. As the name suggested, globular proteins are in spherical structure. Their structure is so different with other proteins’ because they have a very special tertiary structure. The primary structure of globular protein is the same as any other proteins. The primary structure of proteins aims to be the linear structure formed by different amino acids in a peptide chain. Each amino acid is held together with each other by covalent bonds like peptide bonds. The primary structure is formed during the process of biosynthesis or translation. Similarly, the secondary structure of globular protein follows the normal protein secondary structure. Generally, the interacting hydrogen bonds between backbones cause the polypeptides twisted and from two shapes of secondary structure proteins: the (alpha) helix shape and the (beta) pleated sheet. The tertiary structure of globular protein differ it from other kinds of proteins. In globular proteins, polypeptide backbone, which refers to a single polypeptide chin, does fold upon itself. There are mainly four kinds of interactions in globular that hold the amino acid chains together. The first and the most special one is the hydrophobic interaction. Globular is typically soluble in water and polar environment. This is because the hydrophilic amino acids, like serine, are interacting with the polar environment and, therefore, are in the outer side. Vice versa, the hydrophobic amino acids, like alanine, are buried inside the protein. Therefore, the hydrophobic interaction caused the spherical shape of globular protein. Detergent can destroy this interaction. The second interaction is caused by the hydrogen bonds. However, the hydrogen bond here is different from the hydrogen bonds in the secondary structure, in which the hydrogen bonds interact between backbones. In tertiary st