Sensitivity to proteolytic degradation was used to monitor folding of polypeptides in vivo. A correlation between competence for export and lack of stable tertiary structure was established by comparing the kinetics of folding of mutated precursor maltose-binding protein that carries a defective leader peptide with the kinetics of folding of wild-type precursor that is competent for export. It is proposed that during export a kinetic competition exists between productive translocation and folding of precursor intracellularly into a stable conformation that is not compatible with transfer.
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