Stephen J. Hardy

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Fundamental to the function of all molecular chaperones is their amazing ability to selectively and rapidly bind proteins in non-native states. Chaperones modulate a kinetic partitioning among the alternative pathways open to polypeptides within a cell, so that the proper pathway is taken. Here we review studies of SecB, a chaperone in Escherichia coli(More)
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(More)
In this paper we study the assembly, in vivo and in vitro, of a family of hexameric, heat-labile enterotoxins produced by diarrheagenic bacteria. The toxins, which consist of an A subunit and five B subunits, are assembled by a highly coordinated process that ensures secretion of the holotoxin complex. We show that (i) oxidation of cysteine residues in the(More)
The interaction of the chaperone SecB with ribosome-bound polypeptides that are in the process of elongation has been studied using an in vitro protein synthesis system. The binding is characterized by the same properties as those demonstrated for the binding of SecB to full-length proteins that are in nonnative conformation: it is readily reversible and(More)