The central dogma of biology deals with the conversion of DNA into RNA and finally into proteins. Proteins play catalytic roles, structural roles, transport roles, and various other roles in the body. Proteins are made up of long strands of amino acids, this arrangement is known as the primary structure. Groups of amino acids interact with each other and fold into alpha helices and beta sheets. These structures are known as secondary structure, and the structure forms to maximize hydrogen bonds within groups, as well as to expel entropically unfavorable "water cages" from the protein's hydrophobic interior (Kudryashov, 2014). The tertiary structure is the finalized structure of the protein that results from the various intermolecular interactions within and between amino acids. Finally, quaternary structure is the incorporation of large polypeptide chains into a larger protein structure (The Structure of Proteins, 2014). The function of proteins is closely linked to their structure, and serious diseases can occur when protein folding goes wrong. Distorted proteins are known as prions (proteinaceous infectious particles) and play a key role in the pathogenesis of many neurodegenerative diseases (Edenhofer et al, 1996). The term prion was first coined by Dr. Stanley B. Prusiner in 1982. He described his interest in the subject as stemming from an encounter with one of his patients who succumbed to Creutzfeldt-Jakob disease ( a prion disease) in just two months. . He was amazed that a person could have their brain destroyed while their body remained unchanged and no immune response was produced (Prusiner, 1998). The prion protein (PrPC or PrP) is considered a normal cellular protein. However, its normal structure and function in the middle of the paper's topic includes ethics and the scarcity of available data. Biologists like Claudio Soto of the University of Texas Medical Branch at Galveston are pushing ethical boundaries by mass-producing these prions to accelerate progress in this field (Khamsi, 2006). The dangers of mass production of these extremely denaturation-resistant prions are obvious, but he recognizes that the possible gains far outweigh the risks. Another limitation is that it is very difficult to study the progression of these diseases from onset to death in humans, because they are usually not diagnosed until symptoms appear. This leaves a very small window of time to obtain information about humans. Another factor that makes studying these diseases so difficult is that they are extremely rare. Understanding prions has the potential to completely redefine our understanding of proteins.