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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gast K,Damaschun G,Desmadril M,Minard P,Müller-Frohne M,Pfeil W,Zirwer Ddoi
10.1016/0014-5793(94)01437-6subject
Has Abstractpub_date
1995-01-30 00:00:00pages
247-50issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(94)01437-6journal_volume
358pub_type
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