Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein

Destabilization of prion protein induces a conformational change from normal prion protein (PrP(C)) to abnormal prion protein (PrP(SC)). Hydrophobic interaction is the main driving force for protein folding, and critically affects the stability and solvability. To examine the importance of the hydro...

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Detalles Bibliográficos
Autores principales: Lee, Juhwan, Chang, Iksoo, Yu, Wookyung
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6915724/
https://www.ncbi.nlm.nih.gov/pubmed/31844149
http://dx.doi.org/10.1038/s41598-019-55661-2

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6915724/
https://www.ncbi.nlm.nih.gov/pubmed/31844149
http://dx.doi.org/10.1038/s41598-019-55661-2

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