The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60)

Nicholas C. Price, Sharon M. Kelly, Graeme J. Thomson, John R. Coggins, Stephen Wood, Arlene Auf Der Mauer

Research output: Contribution to journalArticlepeer-review

Abstract

The unfolding of the bacterial chaperone protein groEL (cpn60) in solutions of guanidinium chlodire (GdnHCl) has been studied. From the results of CD, fluorescence and light scattering, it is clear that major structural transitions in the protein occur over the range 1.0–1.5 M GdnHCl. The ATPase activity of the protein is lost at lower concentrations (0.75 M). After denaturation in concentrations of GdnHCl above 1.5 M, removal of the denaturing agent by dialysis results in very nearly complete regain of secondary structure (as judged by CD), but not the regain of correct tertiary or quaternary structure, or ATPase activity. The product was shown to be very sensitive to proteolysis by thermolysin, unlike the native protein, and not to show enhanced binding of ANS, a characteristic property of the ‘molten globule’ state of proteins.. The results are discussed in relation to current information concerning the assembly of the groEL protein.
Original languageEnglish
Pages (from-to)52-58
JournalBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume1161
Issue number1
DOIs
Publication statusPublished - 1 Jan 1993

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