The amino acid is a hydrophobic and aromatic essential amino acid. The compound is relatively non-reactive because of the benzene ring in its structure. Since it is nonpolar, the amino acid does not dissolve in water. Due to its hydrophobic nature, the amino acid is buried in the hydrophobic core of protein structures. However, the aromatic side chain in the structure of the amino acid affects protein structure by staking with the aromatic side chains of other amino acids. The side chain of the amino acid is relatively non-reactive and as such is not often involved in the functions of the protein.
The stability of the structure of the proteins at the tertiary level can be attributed to various interactions and bonds. More specifically, the interactions between one R-group and another determines the stability of the structure of the proteins. From the interactions of one R-group and another, different bonds are formed. For instance, hydrogen bonds are formed between the interactions of polar R-groups. The interaction between charged R-groups results in ionic bonds. Additionally, there are hydrophobic interactions between different nonpolar R-groups at the tertiary level of a protein structure. Covalent bonds are also responsible for stability in the protein structure. For instance, the R-groups of certain amino acids, such as cysteine have sulfur atoms. These atoms can bond covalently with other sulfur atoms on different cysteine molecules. The disulfide covalent bond that is formed stabilizes the structure of the proteins at the tertiary level (Vasudevan, Sreekumari & Vaidyanathan, 2013).
Protein misfolding and aggregation has role to play in the occurrence of bovine spongiform encephalopathy. The proteins that fold during the occurrence of bovine spongiform encephalopathy are called prions. The protein misfolds because some of them have unstable structures. The aggregation occurs due to the disruption of the chaperones which serve as the mediators for refolding of proteins. They also degrade proteins that have misfolded in order to avoid aggregation. Prions cause other proteins in a cell to misfold in an abnormal manner. This causes changes in the structure of the proteins. As such, proteins that normally existed in liquid form inside the cell start to solidify. Since most of the damage is in the brain cells, the solidification of the liquid proteins in the brain cells results in the damage of the tissue resulting in coordination difficulties and changes in the behavior of the affected animals (Reynaud, 2010).
Prions have a hand in the occurrence of bovine spongiform encephalopathy. While prions are not largely considered as living things, they are molecules of misfolded proteins. These molecules can propagate inside the cells by transmitting their misfolded protein state to other proteins in the cell. The propagation of the molecules has a role to play in the occurrence of disease conditions. When the molecules enter into a healthy cell, they induce the protein molecules that are properly folded to propagate into the misfolded prion forms. They provide templates through which protein misfolding is based. The newly misfolded proteins (prions) induce other protein molecules to misfold based on the templates, resulting in a chain reaction (Brown, 2005).
The discussion on bovine spongiform encephalopathy has to touch on chaperone proteins at one point. As discussed earlier, bovine spongiform encephalopathy occurs due to the misfolding of proteins. Molecular chaperones act inside the cells to correct the process through which proteins misfold. This is by assisting proteins within the cell to achieve an active three dimensional structure in order to achieve functionality. In achieving this, chaperone proteins prevent protein misfolding and aggregated protein structures. In the presence of chaperone proteins, the efficiency of folding is enhanced why the chaperone proteins influence the dynamics that affect the protein folding process and inhibiting the influence of the aspects and events that result in protein aggregation (Chaudhuri & Subhankar, 2006). Typical chaperone proteins act differently when compared to proteins acting as chaperones. Chaperones that are associated with ribosomes guide the first steps of folding by interaction with the polypeptide chains during the translation phase. The chaperones that are not bound to ribosomes influence the folding process during and after the translation phase (Hoffmann, Bukau & Kramer, 2010).
The effects of bovine spongiform encephalopathy are life threatening, especially because they affect the brain and the nervous system. Additionally, the fact that the disease condition does not have a cure or a vaccine means that prevention strategies are dire. Countries should protect animal health by banning the feeding of ruminants with mammalian proteins. Countries should also include additional prohibitions on other tissues that bear the risk of spreading the prions causing bovine spongiform encephalopathy. The tissues implicated in this recommendation include brain tissues and those found in the spine columns of mammalian animals. This is because these are the tissues that are affected by bovine spongiform encephalopathy. The disposal of animals infected with the prions causing the bovine spongiform encephalopathy is very vital. I recommend the use of incineration to dispose fallen animals. The animals can also be buried after being incinerated.
Brown, D. R. (2005). Neurodegeneration and prion disease. New York, NY: Springer Science+Business Media.
Chaudhuri, T. & Subhankar, P. (2006). Protein-misfolding diseases and chaperone-based therapeutic approaches, Federation of European biochemical societies journal. 1331– 1349
Hoffmann, A., Bukau, B. & Kramer, G. (2010). Structure and function of the molecular chaperone trigger factor. Biochimica et biophysica acta molecular cell research, 1803 (6): 650-661.
Reynaud, E. (2010) Protein Misfolding and Degenerative Diseases. Nature Education 3(9):28
Vasudevan, D. Sreekumari, S. & Vaidyanathan, K. (2013). Textbook of biochemistry for medical students. s.l.: Jaypee brothers medical p.