Abstract
Calmodulin regulates a wide variety of cellular functions by interacting with its binding proteins or enzymes 1. Based on studies with a number of naturally occuring peptides that bind calmodulin with high affinity, it has been predicted that both ionic and hydrophobic interactions are involved in the association and that a general characteristic of a calmodulin-binding peptide is the ability to form a basic, amphiphilic helix 2–5. Indeed as the sequence of calmodulin-binding proteins have become known, the basic, amphiphilic helix has been shown to be the one common feature of the calmodulin-binding domain 6–16.
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© 1989 Plenum Press, New York
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Ono, T., Means, A.R. (1989). Calspermin is a Testis Specific Calmodulin-Binding Protein Closely Related to Ca2+/Calmodulin-Dependent Protein Kinases. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0_29
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DOI: https://doi.org/10.1007/978-1-4684-5679-0_29
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