Prions are misfolded proteins that can convert

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Unformatted text preview: ensional structure of the protein domain in question. As we have discussed, space is directly related to function an evolutionarily conserved domain is likely to be functionally important. Therefore, conserved glycine residues fall at positions where the versatility of a “small” amino acid is necessary for achieving the proper 3-dimensional structure. A good example of the role of glycine in filling up the space is the protein collagen. Certain neurological diseases have been linked to protein infectious agents (“prions”). Explain why study of protein three- dimensional structure and conformational change is essential to understand the underlying disease process. Prions are ‘misfolded’ proteins that can convert properly folded α -helix-rich forms of the protein into the misfolded β -sheet rich form. This alternative protein conformation leads to protein aggregation and cell damage. This is the cause of several neurological disorders in humans and animals, such as Kuru, CJD, Mad-cow disease and Scrapies. Bas...
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