Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus.
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 an...
| Hauptverfasser: | , , , , , |
|---|---|
| Format: | Journal article |
| Sprache: | English |
| Veröffentlicht: |
1996
|