Abstract
Understanding the role of calmodulin (CaM) in calcium signal transduction implies to describe the calcium-dependent molecular mechanism of interaction of CaM with the various CaM-binding domains (CBD). In order to fulfill this aim, we have developed a new strategy and the afferent techniques to quantify the interaction of CaM with any CBD as a function of calcium concentration. Excel software has been used to deconvolute the experimental data and to obtain the macroscopic constants characterizing the system. We are illustrating our approach on six different CaM/CBD. This strategy may be used to analyze the interaction between any calcium-binding protein and its targets.
Emilie Audran and Rania Dagher have contributed equally to the work.
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Acknowledgments
This work has been supported by grant from ANR CAPHE and by CNRS and University of Strasbourg (France). This work has been performed at the technological platform PCBIS (UMS CNRS 3286). S. G is member of this platform.
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Audran, E., Dagher, R., Gioria, S., Kilhoffer, MC., Haiech, J. (2013). New Aspects of Calmodulin–Calmodulin Binding Domains Recognition. In: Heizmann, C. (eds) Calcium-Binding Proteins and RAGE. Methods in Molecular Biology, vol 963. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-230-8_4
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DOI: https://doi.org/10.1007/978-1-62703-230-8_4
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