Unveiling the activation dynamics of a fold-switch bacterial glycosyltransferase by (19)F NMR

Fold-switch pathways remodel the secondary structure topology of proteins in response to the cellular environment. It is a major challenge to understand the dynamics of these folding processes. Here, we conducted an in-depth analysis of the α-helix–to–β-strand and β-strand–to–α-helix transitions and...

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Detalles Bibliográficos
Autores principales: Liebau, Jobst, Tersa, Montse, Trastoy, Beatriz, Patrick, Joan, Rodrigo-Unzueta, Ane, Corzana, Francisco, Sparrman, Tobias, Guerin, Marcelo E., Mäler, Lena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2020
Materias:
Glycobiology and Extracellular Matrices
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7380196/
https://www.ncbi.nlm.nih.gov/pubmed/32434931
http://dx.doi.org/10.1074/jbc.RA120.014162

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7380196/
https://www.ncbi.nlm.nih.gov/pubmed/32434931
http://dx.doi.org/10.1074/jbc.RA120.014162

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