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Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus.

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...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1996.0701

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
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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

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