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- W2118740303 abstract "It has been recently reported through classical molecular dynamics simulations, that potassium ions have lower binding affinity for glutamate residues than water, leading to destabilization of the helical conformations of the peptide. In contrast, sodium ions have much stronger affinity for glutamate groups than for water, strongly stabilizing the helical conformations of the peptide. On the other hand, recent CD and UVRR experiments found that both ions: sodium and potassium, have the same effect, inducing just a very small stabilization on the helical conformations of the polypeptide for concentrations greater than 1M. In this work, we investigate the controversy presented above by performing classical molecular dynamics simulations of the poly-l-glutamate immersed in pure water, sodium chloride and potassium chloride. We present alpha helical contents in each solvent and give a quantitative estimation of how the barrier between alpha helix and unfolded states is affected by the presence of the ions." @default.
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- W2118740303 date "2011-02-01" @default.
- W2118740303 modified "2023-09-30" @default.
- W2118740303 title "Effects of Potassium and Sodium Ions on the Stability of Poly-L-Glutamate" @default.
- W2118740303 doi "https://doi.org/10.1016/j.bpj.2010.12.1350" @default.
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