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• W2058243276 startingPage "4564" @default.
• W2058243276 abstract "Tetracycline repressor (TetR), which constitutes the most common mechanism of bacterial resistance to an antibiotic, is a homodimeric protein composed of two identical subunits, each of which contains a domain possessing a helix–turn–helix motif and a domain responsible for binding tetracycline. Binding of tetracycline in the protein pocket is accompanied by conformational changes in TetR, which abolish the specific interaction between the protein and DNA. Differential scanning calorimetry (DSC) and CD measurements, performed at pH 8.0, were used to observe the thermal denaturation of TetR in the absence and presence of tetracycline. The DSC results show that, in the absence of tetracycline, the thermally induced transitions of TetR can be described as an irreversible process, strongly dependent on scan rate and indicating that the protein denaturation is under kinetic control described by the simple kinetic scheme: , where k is a first‐order kinetic constant, N is the native state, and D is the denatured state. On the other hand, analysis of the scan rate effect on the transitions of TetR in the presence of tetracycline shows that thermal unfolding of the protein can be described by the two‐state model: . In the proposed model, TetR in the presence of tetracycline undergoes co‐operative unfolding, characterized by an enthalpy change (Δ H cal = 1067 kJ·mol −1 ) and an entropy change (Δ S = 3.1 kJ·mol −1 )." @default.
• W2058243276 created "2016-06-24" @default.
• W2058243276 creator A5065863183 @default.
• W2058243276 creator A5091611908 @default.
• W2058243276 date "2003-10-23" @default.
• W2058243276 modified "2023-10-18" @default.
• W2058243276 title "A differential scanning calorimetry study of tetracycline repressor" @default.
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• W2058243276 doi "https://doi.org/10.1046/j.1432-1033.2003.03856.x" @default.
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