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Updated: Jan 21, 2026

Spatial Separation of Molecular Conformers and Clusters
Published on: January 9, 2014
Molecular Dynamics Study of the Changes in Conformation of Calmodulin with Calcium Binding and/or Target Recognition
Hiroshi Kawasaki1, Natsumi Soma2, Robert H Kretsinger3
1Department of Medical Life Science, Graduate School of Medical Life Science, Yokohama City University, Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan. kawasaki@yokohama-cu.ac.jp.
Abstract:
Calmodulin is a calcium binding protein with two lobes, N-lobe and C-lobe, which evolved from duplication and fusion of a single precursor lobe of a pair of EF-hand. These two lobes of calmodulin show subtle differences in calcium binding and target recognition; these are important for the functions of calmodulin. Since the structures, especially main chain conformations, of two EF-lobes in holo-form are quite similar; this is a good example to evaluate the effect of side chains for structural dynamics. We analyzed the structure of calmodulin using molecular dynamics and found differences in conformational ensembles between N- and C-lobes. We also showed the mutant structures created by homology modeling could reproduce the difference of dynamic motion between N- and C-lobes.
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