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  • Title: Specific interaction of the Escherichia coli chaperone GroEL (60-KDA heat shock protein) with the liganded form of the galactose binding protein.
    Author: Richarme G, el Yaagoubi A, de Crouy-Chanel A, Kohiyama M.
    Journal: Biochem Mol Biol Int; 1994 Nov; 34(5):955-61. PubMed ID: 7703912.
    Abstract:
    The Escherichia coli chaperone GroEL interacts more strongly with the liganded form of the galactose binding protein (the galactose binding protein-galactose complex), than with its unliganded form. This specific interaction is reflected by the stimulation of the ATPase activity of GroEL by the liganded galactose binding protein. Interactions between native proteins and chaperones could be more frequent than generally suspected, and may help to detect protein conformational changes.
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