However, the mutated prion protein is insoluble and the protein digestion. Based on these differences, one might expect these two forms of the prion protein to be composed distinctly different sequences of amino acids, but this is not the case. Prions are proteins, a diverse group of macromolecules. Proteins are capable of a wide variety of functions and activities. This is due to the great variety of structures. Proteins are polymers of amino acids known as polypeptides. These amino acids are the structural building blocks of proteins. Amino acids have a single carbon linked to: an amino group, a carboxylic acid group and a side chain. These side chains vary in structure and determine the chemical properties of the amino acids. Each protein has a unique and highly ordered structure that is highly specific with the molecules it interacts with. The assortment of the twenty amino acids are important because of the activities the protein can perform in terms of both the intramolecular interactions and intermolecular interactions. Intramolecular interactions are the forces within a molecule. It could be thought of as intramural collegiate activities, interactions within a molecule. Intermolecular interactions could be thought of as intermediate collegiate activities, interactions outside the molecule and this. During the process of protein synthesis for the normal and mutated prion, special bonds known as peptide bonds form a polypeptide chain. There are several levels of organization that can describe the structure and reactivity of this prion protein. The primary structure is the specific linear sequence of amino acids that constitute the chain. For both the normal and mutated proteins, the primary structure is the same. This sequence of amino acids is very important in both the structure and function of the proteins. Even though the primary structure of any protein is unique, the secondary structure of many different proteins can be the same.