Kinetic studies of the refolding of yeast phosphoglycerate kinase: Comparison with the isolated engineered domains

  • iakas D
  • Betton J
  • Chaffotte A
 et al. 
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Abstract

The role of domains as folding units was investigated with a two-domain protein, yeast phos-phoglycerate kinase. Each of the domains was produced independently by site-directed mutagenesis. It has been previously demonstrated by several criteria that these domains are able to fold in vivo into a quasi-native structure [Minard et al. (1989a) Protein Eng. 3, 55-60; Fairbrother et al. (1989) Protein Eng. 3, 5-1 11. In the present study, the reversibility of the unfolding-refolding process induced by guanidine hydrochloride was investigated for the intact protein and the isolated domains. The transitions were followed by circular dichroism for both domains and the intact protein and by the variations in enzyme activity for the intact protein. Tryptophan residues were used as intrinsic conformational probes of the C-domain. An

Author-supplied keywords

  • domains
  • folding
  • kinetics
  • phosphoglycerate kinase

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