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Although proteins with internal duplications in which the two halves of the protein have opposite orientations in the membrane are quite common among the E. coli inner membrane proteins£¬we conclude that homologs with opposite membrane orientations, as well as proteins with a dual topolgy, are exceedingly rare. Possibly, protein folding and assembly are more efficient when the two oppositely oriented halves are part of a single polypeptide chain than when they aree expressed separately.
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