Met125 is essential for maintaining the structural integrity of calmodulin’s C-terminal domain

We have used NMR and circular dichroism spectroscopy to investigate the structural and dynamic effects of oxidation on calmodulin (CaM), using peroxide and the Met to Gln oximimetic mutations. CaM is a Ca(2+)-sensitive regulatory protein that interacts with numerous targets. Due to its high methioni...

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Detalles Bibliográficos
Autores principales: Nelson, Sarah E. D., Weber, Daniel K., Rebbeck, Robyn T., Cornea, Razvan L., Veglia, Gianluigi, Thomas, David D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7721703/
https://www.ncbi.nlm.nih.gov/pubmed/33288831
http://dx.doi.org/10.1038/s41598-020-78270-w

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7721703/
https://www.ncbi.nlm.nih.gov/pubmed/33288831
http://dx.doi.org/10.1038/s41598-020-78270-w

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