The thermal stability of recoverin depends on calcium binding and its myristoyl moiety as revealed by infrared spectroscopy

Biochemistry
Kim Potvin-FournierMichèle Auger

Abstract

To evaluate the structural stability of recoverin, a member of the neuronal calcium sensor family, the effect of temperature, myristoylation, and calcium:protein molar ratio on its secondary structure has been studied by transmission infrared spectroscopy. On the basis of the data, the protein predominantly adopts α-helical structures (∼50-55%) with turns, unordered structures, and β-sheets at 25 °C. The data show no significant impact of the presence of calcium and myristoylation on secondary structure. It is found that, in the absence of calcium, recoverin denatures and self-aggregates while being heated, with the formation of intermolecular antiparallel β-sheets. The nonmyristoylated protein (Rec-nMyr) exhibits a lower temperature threshold of aggregation and a higher intermolecular β-sheet content at 65 °C than the myristoylated protein (Rec-Myr). The former thus appears to be less thermally stable than the latter. In the presence of excess calcium ions (calcium:protein ratio of 10), the protein is thermally stable up to 65 °C with no significant conformational change, the presence of the myristoyl chain having no effect on the thermal stability of recoverin under these conditions. A decrease in the thermal stability of rec...Continue Reading

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Citations

Apr 25, 2018·European Biophysics Journal : EBJ·Kim Potvin-FournierMichèle Auger
Oct 27, 2018·Langmuir : the ACS Journal of Surfaces and Colloids·Izabella BrandKarl-Wilhelm Koch

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