- Abstract:
-
Thermal unfolding of the small hyperthermophilic DNA-binding protein Sso7d was studied by circular dichroism spectroscopy and differential scanning calorimetry. The unfolding transition can be described by a reversible two state process. Maximum stability was observed in the region between pH 4.5 and 7.0 where Sso7d unfolds with a melting temperature between 370.8 to 371.9 K and an unfolding enthalpy between 62.9 and 65.4 kcal/mol. The heat capacity differences between the native and the heat...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1006/jmbi.1996.0701
-
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- Journal:
- Journal of molecular biology
- Volume:
- 264
- Issue:
- 5
- Pages:
- 1132-1144
- Publication date:
- 1996-12-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:492aef0c-cc03-4103-8cfd-3700ea43aad9
- Source identifiers:
-
375463
- Local pid:
- pubs:375463
- Language:
- English
- Keywords:
- Copyright date:
- 1996
Journal article
Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus.
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