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Dynamics of a truncated prion protein, PrP(113–231), from (15)N NMR relaxation: Order parameters calculated and slow conformational fluctuations localized to a distinct region

Prion diseases are associated with the misfolding of the prion protein (PrP(C)) from a largely α-helical isoform to a β-sheet rich oligomer (PrP(Sc)). Flexibility of the polypeptide could contribute to the ability of PrP(C) to undergo the conformational rearrangement during PrP(C)–PrP(Sc) interactio...

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Detalhes bibliográficos
Main Authors: O'Sullivan, Denis B D, Jones, Christopher E, Abdelraheim, Salama R, Brazier, Marcus W, Toms, Harold, Brown, David R, Viles, John H
Formato: Artigo
Idioma:Inglês
Publicado em: Wiley Subscription Services, Inc., A Wiley Company 2009
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2708060/
https://ncbi.nlm.nih.gov/pubmed/19173221
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.44
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