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• W2039762023 startingPage "79" @default.
• W2039762023 abstract "With the aid of quantum mechanical calculations we investigate the electronic structure of the full length (FL) potassium channel protein, FL-KcsA, in its closed conformation, and the electronic structure of the ClC chloride channel. The results indicate that both ion channels are strongly polarized towards the extracellular region with respect to the membrane mean plane. FL-KcsA possesses an electric dipole moment of magnitude 403 D while ClC has a macrodipole whose magnitude is about five times larger, 1983 D, thereby contributing to differentiate their membrane electric barriers. The dipole vectors of both proteins are aligned along the corresponding n-fold axes. These results suggest that potassium and chloride ion channels are not passive with respect to the movement of ions across the membrane and the ionic motion driven by the electrochemical potential of the membrane might be affected by the electric field of the protein." @default.
• W2039762023 created "2016-06-24" @default.
• W2039762023 creator A5070143245 @default.
• W2039762023 date "2010-06-01" @default.
• W2039762023 modified "2023-10-18" @default.
• W2039762023 title "Macrodipoles of potassium and chloride ion channels as revealed by electronic structure calculations" @default.
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• W2039762023 doi "https://doi.org/10.1016/j.theochem.2010.03.027" @default.
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