In:
FEBS Letters, Wiley, Vol. 358, No. 3 ( 1995-01-30), p. 247-250
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(94)01437-6
Language:
English
Publisher:
Wiley
Publication Date:
1995
detail.hit.zdb_id:
1460391-3
SSG:
12
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