- Abstract:
-
The reversible thermal unfolding of the archaeal histone-like protein Ssh10b from the extremophile Sulfolobus shibatae was studied using differential scanning calorimetry and circular dichroism spectroscopy. Analytical ultracentrifugation and gel filtration showed that Ssh10b is a stable dimer in the pH range 2.5-7.0. Thermal denaturation data fit into a two-state unfolding model, suggesting that the Ssh10 dimer unfolds as a single cooperative unit with a maximal melting temperature of 99.9 d...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.bbrc.2008.06.030
-
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- Journal:
- Biochemical and biophysical research communications
- Volume:
- 373
- Issue:
- 4
- Pages:
- 482-487
- Publication date:
- 2008-09-05
- DOI:
- EISSN:
-
1090-2104
- ISSN:
-
0006-291X
- URN:
-
uuid:ec103939-1bc1-4d6a-8e31-461d1450d4ad
- Source identifiers:
-
94693
- Local pid:
- pubs:94693
- Language:
- English
- Keywords:
- Copyright date:
- 2008
Journal article
Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10.
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