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Journal article

Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10.

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...

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Publication status:
Published

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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

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