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- W2020870160 abstract "Calmodulin is a regulatory protein involved in a variety of cellular calcium-dependent signaling paths. To verify the effects of calcium ion (Ca2+) binding to calmodulin, we have carried out molecular dynamics simulations at 298 K and energy minimizations for Ca2+-bound and Ca2+-free calmodulins. In our work, we have confirmed that the conformational transition between Ca2+-bound and Ca2+-free states occurs more rapidly in the N-terminal half than in the C-terminal half. We have also shown that Ca2+ binding to calmodulin induces the exposure of hydrophobic clefts, which enables interaction with a wide variety of enzymes, whereas the hydrophobic clefts in Ca2+ calmodulin are packed around the central helix. Because of this packing, the binding affinity of Ca2+-free calmodulin with various agents is reduced compared to that of Ca2+-bound calmodulin. The packing of Ca2+-free calmodulin is mainly achieved by helices II and III of the N-terminal half and helices V and VI of the C-terminal half." @default.
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- W2020870160 date "1993-05-01" @default.
- W2020870160 modified "2023-09-27" @default.
- W2020870160 title "Molecular dynamics studies of the Ca2+ binding effect on calmodulin" @default.
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- W2020870160 doi "https://doi.org/10.1016/0022-2860(93)85020-u" @default.
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