Protein Structure

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Biochemistry Task 2 Donna Whittington 000337251 July 22 , 2016 A. (Wolfe 2000) B. (Borges 2014) (Wolfe 2000a) (Wolfe 2000c) (Wolfe 2000b) C. (Hudon­Miller 2012) D. (Hudon­Miller 2012) E. Hydrophobic Interactions: Proteins are composed of amino acids that contain either hydrophilic or hydrophobic R­groups. It is the nature of the interaction of the R­groups in the…show more content…
The normal prion protein structure is believed to consist of a number of flexible coils called alpha helices. In the abnormal form of the protein, some of these helices are stretched out into flat structures called beta sheets. The normal protein is broken down by cellular enzymes called proteases but the abnormal protein shape is resistant to protease and as a result, these prions replicate and are not broken down by proteases and accumulate in brain tissue causing neurological defects. (DeHaven 2016) 2. Role of a Chaperone Protein in BSE Chaperone Proteins act as ushers that make sure that amino acids continue to the next structure phase without folding incorrectly during the folding process. It is believed that BSE acts as a chaperone protein and that is how the disease is spread. The misfolding of protein is hydrophobic inside the cell. In order for the misfolded protein to not be a minority in the cell, it acts as a chaperone protein and converts normal protein into the misfolded protein. This is an irreversible act. The cell recognizes the decreased amount of normal protein and creates more of it, but it is converted to misfolded protein. This happens over and over. Then all the abnormal protein comes together to form a sticky accumulation of plaque called amyloid plaque.
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