Abstract
At one level the prion diseases will be better understood when we have an adequate description of the structural rearrangements which underlie conversion of the cellular form of PrP to the infectious agent. The recent elucidation of the structure of soluble, recombinant PrP by NMR marks an important first stage in this aim and will focus attention on the dynamics of folding of this molecule, in vitro.
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© 1998 Springer Science+Business Media New York
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Clarke, A.R. (1998). Protein Folding and Misfolding. In: Morrison, D.R.O. (eds) Prions and Brain Diseases in Animals and Humans. NATO ASI Series, vol 295. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1896-3_39
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DOI: https://doi.org/10.1007/978-1-4899-1896-3_39
Publisher Name: Springer, Boston, MA
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