A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB - PubMed (original) (raw)
. 1991 Jan 25;251(4992):439-43.
doi: 10.1126/science.1989077.
Affiliations
- PMID: 1989077
- DOI: 10.1126/science.1989077
A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB
S J Hardy et al. Science. 1991.
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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