Forces that stabilize protein in tertiary level.
The tertiary structure contains several protein secondary structures that appears as three-dimensional object due to presence of one polypeptide chainSinauer Associates(2000). The shape come about due to folding of the of the whole protein structure by itself.
The stability and three-dimensional shape of the tertiary structure is due to forces or bond that exists between it as are held together by side chains. The force are as follows:-
Non-Polar Hydrophobic Interactions or Dispersion forces- the electrons in the protein structure are evenly distributed that are in different atoms. The non-polar atoms tend to repel the polar material and water making them to evenly distribute and having interactions to each other. The bonding created from non-polar atoms is essential for the stabilization of the bond in the tertiary structure.
Ionic bonding- the protein is made up of amino acids that are charged to form its structure. The charges can either be positive or negative depending with the amino acid type. There is always an attraction between the positive charges and negative charges which make the oppositely charged amino acids to attract each other by the side.
Hydrogen bonding- the amino acids in the protein structure contain oxygen atom, nitrogen atom and hydrogen atom. The hydrogen atom is normally found inside either the nitrogen atom or oxygen atom and the atoms normally contain charges due to the ions present in them. When the oxygen atom is extremely charged negatively it will tend to attract another oxygen atom that has hydrogen atom as its component as that makes it positively charged. This same law of interactions may also apply to the nitrogen atom and this is what creates the bond.
Disulfide linkages- the protein structure contains molecules and the three-dimensional tertiary structure is formed as result of folding of the protein the amino acids in it are brought together. The folding brings about linking and oxidation inside the protein structure. When the sulfhydryl group are oxidized they result to formation of cysteine which forms the stability and bonding.
Roles of prions in BSE.
The proteinaceous infectious particle are proteins that are normally found in the physical cover that surrounds the cellMegansimmer (2003). Its usually referred to as a disease causing micro-organism that causes the transmissible spongiform encephalopathies diseaseRobertson(2012). The prions are normally proteins and are also subject to undergo folding to lead to the formation of three-dimension like structures. The prions however are proteins that undergo abnormal folding like unfinished folding or unfolding Kupfer,Hinrichs, and Groschup (2009).
Misfolding occurs when the proteins fail to fold correctly which is in most cases brought about by complications or failure of chaperones proteins to act as required. The misfolded proteins are the ones that accumulate to form an aggregation that lead to the amyloid plague. The aggregation is related to unfolding in the sense it can only occur when a protein has not folded as required. When all the proteins have folded to form the protein structure correctly there can never be aggregation.
The prions are just proteins that like others can undergo the folding. The prions are those proteins that have undergone folding but due to certain circumstancesthey have misfoldedor completely which leads to incorrect formation of the protein structure. The unfolded proteinswhich are prions can aggregate as the numbers increase in the same cell. This aggregation brings about the structures that have not formed as expected and causing certain abnormalities. The abnormalities that arise are the one that can lead to the disease.
Role of proteins chaperone in BSE.
Chaperone are proteins that are found in all cells in the body involved in different functions of the body. The main function of the chaperone proteins are to hold tightly the wrongly folded and unfolded polypeptides that are responsible for forming the three-dimensional protein structure especially in the tertiary level. The chaperone proteins act as facilitators of the folding of other proteins by being catalyst in the process in which the proteins are being. They are considered catalyst to mean they are not folded during the process and cannot be found in the final product after folding which is the protein structure. The presence of chaperones ensures the stabilization of the polypeptides to prevent aggregation due to incorrect folding in the cells.
Chaperone proteins are catalysts of protein folding ensuring proper folding to make the three-dimensional structure. In normal cases the cell must have both folded and incorrectly folded proteins but the improper folded proteins are very less reason being the chaperone always tries to ensure all proteins are folded. The unfolded proteins due to less numbers and increasing their numbers will act as chaperone and convert the correctly folded proteins to be unfolded. This process done in a permanent ordeal in that the normal folded proteins changed to unfolded can never return to their previous state. The cell will ensure the number of normal folded proteins are as required by manufacturing more while they are being converted to unfolded proteins. The unfolded proteins will now undergo aggregation to form a distress that may contribute to Bovine Spongiform EncephalopathyHollyann Fulkerson (2014).
Recommendations to decrease risk of transmission of BSE.
Conducting test for Bovine Spongiform Encephalopathy can in animal meat before its distribution and consumption by consumers can be one essential practice for controlling its spread. There are body parts that are affected by the Bovine Spongiform Encephalopathy the best way to control it being transmitted to individuals would be to removing those parts when its being prepared for processing and consumption. The part can include the brain which is normally affected by the disease.
Fulkerson H. (2014).Introduction to proteins, their structures, misfolding, and prevention.BSE 101
Kupfer L., Hinrichs W. and Groschup M. (2009). National Institutes of HealthPrion Protein
Misfolding.US National Library of Medicine.
Sinauer Associates (2000). The Cell: A Molecular Approach. 2nd edition.
Robertson S. (2012).What is a Prion?
Available at: http://www.news-medical.net/health/Whatis-a-Prion.aspx.(Accessed: 17th October 2016)
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