Selective observation of semi-rigid non-core residues in dynamically complex mutant huntingtin protein fibrils

Many amyloid-forming proteins, which are normally intrinsically disordered, undergo a disorder-to-order transition to form fibrils with a rigid β-sheet core flanked by disordered domains. Solid-state NMR (ssNMR) and cryogenic electron microscopy (cryoEM) excel at resolving the rigid structures withi...

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Detalles Bibliográficos
Autores principales: Matlahov, Irina, Boatz, Jennifer C., van der Wel, Patrick C.A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Advances in biomolecular structure and dynamics elucidation by solid-state NMR
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9677204/
https://www.ncbi.nlm.nih.gov/pubmed/36419510
http://dx.doi.org/10.1016/j.yjsbx.2022.100077

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9677204/
https://www.ncbi.nlm.nih.gov/pubmed/36419510
http://dx.doi.org/10.1016/j.yjsbx.2022.100077

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