Abstract
Calbindin D9k constitutes an attractive model system for exploring the relationships between structure, dynamics and function in the EF-hand family of proteins. It is the smallest protein known (Mr ≈ 8,500; 75 a.a:s) with a pair of EF-hand Ca2+-binding sites and its structure resembles closely the globular domains of the homologous proteins calmodulin, parvalbumin and skeletal muscle troponin C. [1,7]. The schematic structure of calbindin is shown in Fig. 1.
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© 1989 Plenum Press, New York
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Forsén, S. et al. (1989). Neutralization of Surface Charges Markedly Affects the Properties of Bovine Calbindin D9k . 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_20
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DOI: https://doi.org/10.1007/978-1-4684-5679-0_20
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