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- W2026302783 abstract "With advancement in computing hardware and simulation techniques scientists have developed a substantial overlap between the timescales accessible to atomic-level simulations and those on which the fastest-biological actions take place. In this work we probe the temperature dependent behavior of Calmodulin (CaM) protein using Molecular dynamics (MD). CaM plays an important role in calcium signaling pathways in the eukaryotic cells as it can bind to a variety of other proteins or small organic compounds. Environmental conditions such as temperature would play an important role in the dynamics of this protein. Earlier such kinds of studies have been performed experimentally using fluorescence measurements as in. The calcium bound form of the protein CaM is observed to undergo a reversible conformation change in the temperature range 22-28°C. Leap-dynamics approach was used earlier to study the temperature dependent conformation change of CaM. In this work we perform extensive MD simulations of 100 ns each at various temperatures ranging 280-360 K on the 3CLN and 1CFD forms of calmodulin. A remarkable dependence of folding and unfolding on the temperature and initial structure is obtained similar to as reported in our earlier study. The linker is observed to be more flexible in the case of 1CFD leading to a bend compact form during the simulation at 325 K. 3CLN on the other hand tries to remain in a state close to its initial extended structure. Normal mode analysis is also performed to understand the type of motion experienced by the protein during the MD simulation." @default.
- W2026302783 created "2016-06-24" @default.
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- W2026302783 date "2015-01-01" @default.
- W2026302783 modified "2023-09-28" @default.
- W2026302783 title "Probing Temperature Dependent Conformation Change of Calmodulin Protein using Molecular Dynamics Simulations" @default.
- W2026302783 doi "https://doi.org/10.1016/j.bpj.2014.11.286" @default.
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