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• W2087458839 abstract "The topology of hydrophobic intramembrane proteins is characterized by a statistical asymmetry in the distribution of positively-charged residues on the two sides of the membrane, the 'inside- or cis-positive rule'. A mechanism is proposed involving only neutral residue transfer. For a tightly bound polypeptide adsorbed on the membrane and not at equilibrium, the pK values of the ionic residues related to dissociation of the proton into the aqueous phase bulk are increased because of interaction with the negative charges at the membrane surface. The pK shift would selectively neutralize aspartate and glutamate residues, favoring their translocation across the membrane, while stabilizing the impermeant positively charged state of lysine and arginine residues." @default.
• W2087458839 created "2016-06-24" @default.
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• W2087458839 date "1995-08-07" @default.
• W2087458839 modified "2023-10-15" @default.
• W2087458839 title "On the physical basis for the <i>cis</i>‐positive rule describing protein orientation in biological membranes" @default.
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• W2087458839 doi "https://doi.org/10.1016/0014-5793(95)00756-y" @default.
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