Cold denaturation of yeast phosphoglycerate kinase: which domain is more stable?

FEBS Lett. 1995 Jan 30;358(3):247-50. doi: 10.1016/0014-5793(94)01437-6.

Abstract

Under destabilising conditions both heat and cold denaturation of yeast phosphoglycerate kinase (PGK) can be observed. According to previous interpretation of experimental data and theoretical calculations, the C-terminal domain should be more stable than the N-terminal domain at all temperatures. We report on thermal unfolding experiments with PGK and its isolated domains, which give rise to a revision of this view. While the C-terminal domain is indeed the more stable one on heating, it reveals lower stability in the cold. These findings are of importance, because PGK has been frequently used as a model for protein folding and mutual domain interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calorimetry, Differential Scanning
  • Circular Dichroism
  • Cold Temperature
  • Enzyme Stability
  • Phosphoglycerate Kinase / chemistry*
  • Protein Denaturation
  • Saccharomyces cerevisiae / enzymology*
  • Spectrophotometry, Ultraviolet

Substances

  • Phosphoglycerate Kinase