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Updated: Jul 31, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Ca2+ binding sites in calmodulin and troponin C alter interhelical angle movements
Kunihiko Goto1, Akira Toyama, Hideo Takeuchi
1Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, IL 60611-3008, USA. kunihigoto@aol.com
Abstract:
Molecular dynamics analyses were performed to examine conformational changes in the C-domain of calmodulin and the N-domain of troponin C induced by binding of Ca(2+) ions. Analyses of conformational changes in calmodulin and troponin C indicated that the shortening of the distance between Ca(2+) ions and Ca(2+) binding sites of helices caused widening of the distance between Ca(2+) binding sites of helices on opposite sides, while the hydrophobic side chains in the center of helices hardly moved due to their steric hindrance. This conformational change acts as the clothespin mechanism.
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