The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

Many proteins have the potential to aggregate into amyloid fibrils, protein polymers associated with a wide range of human disorders such as Alzheimer’s and Parkinson’s disease. The thermodynamic stability of amyloid fibrils, in contrast to that of folded proteins, is not well understood: the balanc...

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Detalles Bibliográficos
Autores principales: van Gils, Juami Hermine Mariama, van Dijk, Erik, Peduzzo, Alessia, Hofmann, Alexander, Vettore, Nicola, Schützmann, Marie P., Groth, Georg, Mouhib, Halima, Otzen, Daniel E., Buell, Alexander K., Abeln, Sanne
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2020
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7282669/
https://www.ncbi.nlm.nih.gov/pubmed/32365068
http://dx.doi.org/10.1371/journal.pcbi.1007767

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7282669/
https://www.ncbi.nlm.nih.gov/pubmed/32365068
http://dx.doi.org/10.1371/journal.pcbi.1007767

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