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Article

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

Scientific reports - 7 Dec 2020

Nelson Sarah E D, Weber Daniel K, Rebbeck Robyn T, Cornea Razvan L, Veglia Gianluigi, Thomas David D

Abstract excerpt

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 methionine content, CaM is highly susceptible to oxidation by reactive oxygen species under conditions of cell stress and...

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Identifiers

PMID: 33288831
DOI: 10.1038/s41598-020-78270-w
PMCID: PMC7721703

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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