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Cation binding mode of fully oxidised calmodulin explained by the unfolding of the apostate

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
1570-9639
Publisher
Elsevier
Publication Date
Volume
1600
Identifiers
DOI: 10.1016/s1570-9639(02)00450-8
Keywords
  • Calmodulin
  • Oxidation
  • Calcium
  • Magnesium
  • Calorimetry
Disciplines
  • Biology

Abstract

Abstract Calmodulin is the most ubiquitous calcium binding protein. The protein is very sensitive to oxidation and this modification has pronounced effects on calmodulin function. In this work, we decided to fully oxidise calmodulin in order to study the consequences on cation binding, domain stability, and α helicity. Oxidation of methionines unfolds completely the apostate of the protein, which upon calcium binding recovers the major part of its secondary and tertiary structure. However, the unstructuring of the apostate results in a protein that binds calcium to any site in an independent manner, does not bind magnesium and does not possess auxiliary sites anymore.

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