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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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Main Authors: | , , , , , , |
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Formato: | Artigo |
Idioma: | Inglês |
Publicado em: |
Wiley Subscription Services, Inc., A Wiley Company
2009
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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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