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Calmodulin (CaM) binds to the membrane‐proximal cytosolic C‐terminal domain of CaV1.2 (residues 1520–1669, CT(1520–1669)) and causes Ca2+‐induced conformational changes that promote Ca2+‐dependent channel inactivation (CDI). We report biophysical studies that probe the structural interaction between CT(1520–1669) and CaM. The recombinantly expressed CT(1520–1669) is insoluble, but can be solubilized...
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