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


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. Study holds ProTherm entries: 9841 Extra Details: additive : DTT(1 mM), protein folding; cold denaturation; domain interaction;,circular dichroism; differential scanning; calorimetry

Submission Details

ID: CCAioopK3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:38 p.m.

Version: 1

Publication Details
Gast K;Damaschun G;Desmadril M;Minard P;Müller-Frohne M;Pfeil W;Zirwer D,FEBS Lett. (1995) Cold denaturation of yeast phosphoglycerate kinase: which domain is more stable? PMID:7843410
Additional Information

Sequence Assay Result Units