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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

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:11

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We have studied the stability of the histone-like, DNA-binding protein HU from the hyperthermophilic eubacteriumThermotoga maritimaand its E34D mutant by differential scanningmicrocalorimetry and CDunder acidic conditions at various concentrations within the range of 2–225lMof monomer. The thermal unfolding of both proteins is highly reversible and clearly follows a two-state dissociation/unfolding model from the folded, dimeric state to the unfolded, monomericone.

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Nội dung Text: 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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