A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB |
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Authors: | S J Hardy L L Randall |
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Institution: | Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660. |
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Abstract: | An in vitro assay for the interaction of SecB, a molecular chaperone from Escherichia coli, with polypeptide ligands was established based on the ability of SecB to block the refolding of denatured maltose-binding protein. Competition experiments show that SecB binds selectively to nonnative proteins with high affinity and without specificity for a particular sequence of amino acids. It is proposed that selectivity in binding is due to a kinetic partitioning of polypeptides between folding and association with SecB. |
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