Because calmodulin activates many different effectors (e.g., protein kinases, phosphodiesterases, calcium transport proteins), a calmodulin molecule must have many different binding sites on its surface. Would you agree with this statement? Why or why not?
No, Calmodulin is a small highly conserved protein 148 amino acids long whose structure is highly conserved throughout eukaryotic kingdom. Such a molecule is unlikely to have different binding sites. But its structure provides it flexibilty to bind to different molecules. It has different non polar grooves in it structure that are non specific in nature. Thus these grooves can bind to different effectors without requiring to have any special sequence of amino acids in these effectors.
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