Abstract
The protein actin is a major constituent of the cytoskeleton of virtually all eukaryotic cells. The relatively stable actin filament structure of muscle cells is essential to muscle contraction; the motile events of non-muscle cells involve active reorganization of the actin filament network. Actin has binding sites for one tightly bound divalent cation and one adenosine nucleotide per molecule. These ligands are important to the stability of the actin molecule and actin filament, and to the ATP hydrolysis that is involved in actin polymerization in a way which is still incompletely understood.
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© 1994 Springer Science+Business Media New York
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Gershman, L.C., Selden, L.A., Kinosian, H.J., Estes, J.E. (1994). Actin-Bound Nucleotide/Divalent Cation Interactions. In: Estes, J.E., Higgins, P.J. (eds) Actin. Advances in Experimental Medicine and Biology, vol 358. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2578-3_4
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DOI: https://doi.org/10.1007/978-1-4615-2578-3_4
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