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Article

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Accepted version

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2019-05-01

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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/187781

Toward understanding calmodulin plasticity by molecular dynamics

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Related resource

https://doi.org/10.4155/fmc-2018-0323

Abstract

Aim: Calmodulin interacts in many different ways with its ligands. We aim to shed light on its plasticity analysing the changes followed by the linker region and the relative position of the lobes using conventional Molecular Dynamics (cMD), accelerated MD (aMD) and scaled MD (sMD). Materials & Methods: Three different structures of calmodulin are compared, obtaining a total of 2.5 μs of molecular dynamics, which have been analysed using the principal component analysis and clustering methodologies Results: sMD simulations reach conformations that cMD is not able to, without compromising the stability of the protein. On the other hand, aMD requires optimization of the setup parameters to be useful. Conclusion: SMD is useful to study flexible proteins, highlighting those factors that justify its promiscuity

Subject

Dinàmica molecular, Calmodulina

Subject (English)

Molecular dynamics, Calmodulin

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Articles publicats en revistes (Ciència dels Materials i Química Física)

Citation

GARRIDO, Eduardo, et al. Toward understanding calmodulin plasticity by molecular dynamics. Future Medicinal Chemistry. 2019. Vol. 11, num. 9, pags. 975-991. ISSN 1756-8919. [consulted: 9 of August of 2026]. Available at: https://hdl.handle.net/2445/187781

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