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

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

Abstract 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 Ca2+-sensitive regulatory protein that interacts with numerous targets. Due to its high m...

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Autores principales: Sarah E. D. Nelson, Daniel K. Weber, Robyn T. Rebbeck, Razvan L. Cornea, Gianluigi Veglia, David D. Thomas
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
Materias:
Medicine
R
Science
Q
Acceso en línea:https://doaj.org/article/36f3e28887f142c5b2edc2e310a92fe1
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