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- W2079682259 abstract "The ionization states of the acidic residues around the Ca2+-binding sites of sarcoplasmic reticulum Ca2+ ATPase are studied by continuum electrostatic calculations and all-atom molecular dynamics simulations with explicit solvent and phospholipids. The two methods consistently indicate that Glu58 and Glu908 are protonated at neutral pH. The Ca2+ coordination and the H-bonds formed by the protonation of Glu58 and Glu908 are stable in an MD simulation, whereas the H-bonds are disrupted and the Ca2+ coordination geometry is severely altered in another simulation treating these residues unprotonated. The results clearly indicate that the H-bonds formed by protonation of Glu58 and Glu908 provide extra stability for the Ca2+-binding sites of Ca2+ ATPase." @default.
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- W2079682259 date "2005-04-07" @default.
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- W2079682259 title "Protonation of the Acidic Residues in the Transmembrane Cation-Binding Sites of the Ca<sup>2+</sup> Pump" @default.
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- W2079682259 doi "https://doi.org/10.1021/ja0427505" @default.
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