NMR characterization of the pH 4 β-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility

Prion diseases are associated with the misfolding of the PrP (prion protein) from a largely α-helical isoform to a β-sheet-rich oligomer. CD has shown that lowering the pH to 4 under mildly denaturing conditions causes recombinant PrP to convert from an α-helical protein into one that contains a hig...

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Detalhes bibliográficos
Main Authors: O'Sullivan, Denis B. D., Jones, Christopher E., Abdelraheim, Salama R., Thompsett, Andrew R., Brazier, Marcus W., Toms, Harold, Brown, David R., Viles, John H.
Formato: Artigo
Idioma:Inglês
Publicado em: Portland Press Ltd. 2006
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1820806/
https://ncbi.nlm.nih.gov/pubmed/16958619
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20060668
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