Báo cáo khoa học: Thermodynamic analysis of the unfolding and stability of the dimeric DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima and its E34D mutant
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We have studied the stability of the histone-like,DNA-binding protein HU from the hyperthermophiliceubacteriumThermotoga maritimaand its E34D mutant bydifferential scanningmicrocalorimetry and CDunder acidicconditions at various concentrations within the range of2–225lMof monomer. The thermal unfolding of bothproteins is highly reversible and clearly follows a two-statedissociation/unfolding model from the folded, dimeric stateto the unfolded, monomericone.
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Báo cáo khoa học: Thermodynamic analysis of the unfolding and stability of the dimeric DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima and its E34D mutant
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Thermodynamic analysis of the unfolding and stability of the dimeric DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima and its E34D mutant
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