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Storage protein of egg white. Lack protease inhibitory activity. The signal sequence is not cleaved. The functional signal for membrane translocation of ovalbumin becomes accessible when the nascent chain is 50 to 60 residues long. The hydrophobic sequence which lies between residues 27 and 43 folds back on the preceding residues to form an amphipathic hairpin structure which is the signal element recognized by the membrane.
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