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Dynamic motion of helix A in the amino-terminal domain of calmodulin is stabilized upon calcium activation

, : Dynamic motion of helix A in the amino-terminal domain of calmodulin is stabilized upon calcium activation. Biochemistry 44(3): 905-914

Calcium-dependent changes in the internal dynamics and average structures of the opposing globular domains of calmodulin (CaM), as well as their relative spatial arrangement, contribute to the productive association between CaM and a range of different target proteins, affecting their functional activation.


PMID: 15654746

DOI: 10.1021/bi048332u

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