Prion diseases are fatal neurodegenerative disorders caused by an aberrant accumulation of the misfolded cellular prion protein (PrPC) conformer, denoted as infectious scrapie isoform (PrPSc). The slow and fast motion models of huPrP and huPrP (E200K) structures were analyzed with the GNM in this paper. It can be seen that the largest fluctuation values corresponding to the helix 1. Residue 147 and residue 150 play an important role in the stability of the helix 1. The major consequence of the E200K substitution appears to be the redistribution of surface charges, resulting in an altered electrostatic potential in the mutant protein. This change is likely to affect the stability of the helix 1. Thus, their behavior might reflect that of wild-type PrP or that of mutants associated with transmissible forms of the disease.
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