Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis

Structural investigations of amyloid fibrils often rely on heterologous bacterial overexpression of the protein of interest. Due to their inherent hydrophobicity and tendency to aggregate as inclusion bodies, many amyloid proteins are challenging to express in bacterial systems. Cell-free protein ex...

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Detalles Bibliográficos
Autores principales: Lends, Alons, Daskalov, Asen, Maleckis, Ansis, Delamare, Aline, Berbon, Mélanie, Grélard, Axelle, Morvan, Estelle, Shenoy, Jayakrishna, Dutour, Antoine, Tolchard, James, Noubhani, Abdelmajid, Giraud, Marie-France, Sanchez, Corinne, Habenstein, Birgit, Guichard, Gilles, Compain, Guillaume, Jaudzems, Kristaps, Saupe, Sven J., Loquet, Antoine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9646696/
https://www.ncbi.nlm.nih.gov/pubmed/36352173
http://dx.doi.org/10.1038/s42003-022-04175-1

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9646696/
https://www.ncbi.nlm.nih.gov/pubmed/36352173
http://dx.doi.org/10.1038/s42003-022-04175-1

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