[[abstract]]Prions are infectious pathogens that cause a group of fatal neuro- degenerative diseases. Prion diseases can be infectious, sporadic and genetic mutation. The infectious forms of these diseases including bovine spongiform encephalopathy (BSE), Crutzfeldt-Jakob disease (CJD), scrapie of sheep, and Alzheimer`s disease, are usually characterized by the accumulation in the brain of the transmissible pathogen, an abnormally folded prion protein (PrP) termed PrPsc. PrPsc is the isoform of the normal, cellular PrP termed PrPc. However, some inherited PrP mutations appear to cause neurodegeneration in the absence of PrPsc, instead of a transmembrane form of PrP termed ctmPrP. At present, neither the relationship between the neurodegeneration and ctmPrP nor the conformation of ctmPrP has remained clear. In our simulation, we have designed a sequence composed of 25 amino acids in 3D lattice model to simulate the transformation of TM1 in the endoplasmic reticulum membrane. Furthermore, we also have simulated the correlation between the concentration of PrP and folding time. To insure that our simulations models are correct, we have compared our results with Prusiner’s incubation times of the experiments on transgenic mice.
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