Essay On Misshapen Proteins

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The central dogma of biology deals with the conversion of DNA to RNA and finally into proteins. Proteins play catalytic roles, structural roles, transport roles and a variety of other roles in the body. Proteins are made of long strands of amino acids, this arrangement is known as its primary structure. The amino acid groups interact with each other and fold into alpha helices and beta sheets. These structures are known as its secondary structure, and the structure forms to maximize hydrogen bonding within groups, as well as to expel entropically unfavorable “water cages” from the hydrophobic interior of the protein (Kudryashov, 2014). The tertiary structure is the finalized structure of the protein that arises from the various intermolecular interactions within and between the amino acids. Finally, the quaternary structure is the incorporation of large polypeptide chains into a larger protein structure (The Structure of Proteins, 2014). Protein function is intertwined with its structure, and severe illnesses can arise when protein folding goes awry. Misshapen proteins are known as prions (proteinaceous infectious particle), and they are key 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 topic as stemming from an encounter with a patient of his that succumbed to Creutzfeldt-Jakob disease (a prion diseases) in a mere two months. He was amazed that a person could have their brain destroyed while their body remained unaffected, 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 paper ... ...s topic include the ethics and the scarcity of data available. Biologists like Claudio Soto, of the University of Texas Medical Branch in Galveston, are pushing the ethical boundaries by mass-producing these prions to accelerate gains in this field (Khamsi, 2006). The dangers of mass-producing these prions that are extremely resistant to denaturation 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 inception to death in humans, as they usually go undiagnosed until symptoms start. This leaves a very small window of time in which to gain information in humans. Another factor that makes studying these diseases so difficult is that they are extremely rare. Prion understanding has the potential to completely redefine our understanding of proteins.

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