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Abstract
Porins form water-filled, voltage-controlled channels across bacterial outer membranes. The trimeric protein resides within the hydrophobic membrane domain with unusual stability despite its hydrophilicity. Its channels are formed by β-barrels (one per monomer) that consist of single antiparallel pleated sheets. This motif is found over a considerable evolutionary distance. The general significance of this folding pattern in membrane proteins can only be evaluated once more high-resolution structures have been determined.
Published Version
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