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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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Enregistré dans:
Détails bibliographiques
Publié dans:Sci Rep
Auteurs principaux: Nelson, Sarah E. D., Weber, Daniel K., Rebbeck, Robyn T., Cornea, Razvan L., Veglia, Gianluigi, Thomas, David D.
Format: Artigo
Langue:Inglês
Publié: Nature Publishing Group UK 2020
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC7721703/
https://ncbi.nlm.nih.gov/pubmed/33288831
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-020-78270-w
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