Cold denaturation of yeast phosphoglycerate kinase: which domain is more stable?
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.
Max-Delbrück-Center for Molecular Medicine, Berlin, Germany.
K
K
Gast
G
G
Damaschun
M
M
Desmadril
P
P
Minard
M
M
Müller-Frohne
W
W
Pfeil
D
D
Zirwer
D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D003080:Cold Temperature; D004795:Enzyme Stability; D010735:Phosphoglycerate Kinase / Q000737:chemistry*; D011489:Protein Denaturation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet
D010735:Phosphoglycerate Kinase