Under destabilising conditions both heat and cold denaturation of yeas
t 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 importa
nce, because PGK has been frequently used as a model for protein foldi
ng and mutual domain interactions.