High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry

Proteins require an optimal balance of conformational flexibility and stability in their native environment to ensure their biological functions. A striking example is spidroins, spider silk proteins, which are stored at extremely high concentrations in soluble form, yet undergo amyloid‐like aggrega...

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Detalles Bibliográficos
Autores principales: Kaldmäe, Margit, Leppert, Axel, Chen, Gefei, Sarr, Medoune, Sahin, Cagla, Nordling, Kerstin, Kronqvist, Nina, Gonzalvo‐Ulla, Marta, Fritz, Nicolas, Abelein, Axel, Laίn, Sonia, Biverstål, Henrik, Jörnvall, Hans, Lane, David P., Rising, Anna, Johansson, Jan, Landreh, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Original Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7383493/
https://www.ncbi.nlm.nih.gov/pubmed/31815338
http://dx.doi.org/10.1111/febs.15169

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7383493/
https://www.ncbi.nlm.nih.gov/pubmed/31815338
http://dx.doi.org/10.1111/febs.15169

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