Abstract
Calcium has many biological functions and several groups of macromolecules have the ability to bind calcium with various selectivities and affinities. A rapidly expanding body of knowledge about the structure, thermodynamic and kinetic properties, and cell biology of calcium binding proteins strongly indicates that the targets or receptors for calcium acting as a signal transducer in eukaryotic cells are a class of calcium binding proteins referred to as calcium modulated proteins. These proteins are characterized by their ability to bind calcium in a reversible manner with dissociation constants in the nanomolar to micromolar range under physiological conditions. Although it is not possible yet to predict with any degree of certainty what type of calcium binding structure or molecular mechanism might be associated with a given biological function of calcium, a trend has begun to emerge from the detailed analyses of calcium modulated proteins1
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© 1986 Plenum Press, New York
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Roberts, D.M., Lukas, T.J., Harrington, H.M., Watterson, D.M. (1986). Molecular Mechanisms of Calmodulin Action. In: Trewavas, A.J. (eds) Molecular and Cellular Aspects of Calcium in Plant Development. NATO ASI Series, vol 104. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2177-4_2
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DOI: https://doi.org/10.1007/978-1-4613-2177-4_2
Publisher Name: Springer, Boston, MA
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