Lafitte Daniel, Tsvetkov Philippe O, Devred François, Toci René, Barras Frédéric, Briand Claudette, Makarov Alexander A, Haiech Jacques
UMR CNRS 6032, UFR de Pharmacie, 27 Bd Jean Moulin 13385 Cedex 5, Marseilles, France.
Biochim Biophys Acta. 2002 Nov 4;1600(1-2):105-10. doi: 10.1016/s1570-9639(02)00450-8.
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 alpha 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.
钙调蛋白是最普遍存在的钙结合蛋白。该蛋白对氧化非常敏感，这种修饰对钙调蛋白的功能有显著影响。在这项工作中，我们决定将钙调蛋白完全氧化，以研究其对阳离子结合、结构域稳定性和α螺旋度的影响。甲硫氨酸的氧化使该蛋白的脱辅基状态完全展开，在结合钙后，其二级和三级结构的大部分得以恢复。然而，脱辅基状态的解折叠导致一种蛋白，它能以独立的方式将钙结合到任何位点，不结合镁，也不再拥有辅助位点。
