Zuegg, J.; Gready, Jill
Molecular dynamics simulations have been used to investigate the dynamical and structural behavior of a homology model of human prion protein HuPrP(90-230) generated from the NMR structure of the Syrian hamster prion protein ShPrP(90-231) and of ShPrP(90-231) itself. These PrPs have a large number of charged residues on the protein surface. At the simulation pH 7, HuPrP(90-230) has a net charge of - 1 eu from 15 positively and 14 negatively charged residues. Simulations for both PrPs, using the...[Show more]
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