Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid Protofibrils

Despite numerous studies, a detailed description of the transthyretin (TTR) self-assembly mechanism and fibril structure in TTR amyloidoses remains unresolved. Here, using a combination of primarily small -angle X-ray scattering (SAXS) and hydrogen exchange mass spectrometry (HXMS) analysis, we desc...

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Detalles Bibliográficos
Autores principales: Groenning, Minna, Campos, Raul I., Hirschberg, Daniel, Hammarström, Per, Vestergaard, Bente
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4480009/
https://www.ncbi.nlm.nih.gov/pubmed/26108284
http://dx.doi.org/10.1038/srep11443

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4480009/
https://www.ncbi.nlm.nih.gov/pubmed/26108284
http://dx.doi.org/10.1038/srep11443

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