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• W2137671011 abstract "Abstract The solution structure, thermodynamic stability and hydrodynamic properties of the 55-residue C-terminal domain of UvrB that interacts with UvrC during excision repair in E. coli have been determined using a combination of high resolution NMR, ultracentrifugation, 15N NMR relaxation, gel permeation, NMR diffusion, circular dichroism and differential scanning calorimetry. The subunit molecular weight is 7,438 kDa., compared with 14.5±1.0 kDa. determined by equilibrium sedimentation, indicating a dimeric structure. The structure determined from NMR showed a stable dimer of anti-parallel helical hairpins that associate in an unusual manner, with a small and hydrophobic interface. The Stokes radius of the protein decreases from a high plateau value (ca. 22 Å) at protein concentrations greater than 4 μM to about 18 Å at concentrations less than 0.1 μM. The concentration and temperature-dependence of the far UV circular dichroism show that the protein is thermally stable (Tm ca. 71.5 °C at 36 μM). The simplest model consistent with these data was a dimer dissociating into folded monomers that then unfolds co-operatively. The van't Hoff enthalpy and dissociation constant for both transition was derived by fitting, with ΔH1≈23 kJ mol−1, K1(298)=0.4 μM and ΔH2=184 kJ mol−1. This is in good agreement with direct calorimetric analysis of the thermal unfolding of the protein, which gave a calorimetric enthalpy change of 181 kJ mol−1 and a van't Hoff enthalpy change of 354 kJ mol−1, confirming the dimer to monomer unfolding. The thermodynamic data can be reconciled with the observed mode of dimerisation. 15N NMR relaxation measurements at 14.1 T and 11.75 T confirmed that the protein behaves as an asymmetric dimer at mM concentrations, with a flexible N-terminal linker for attachment to the remainder of the UvrB protein. The role of dimerisation of this domain in the excision repair mechanism is discussed." @default.
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• W2137671011 date "2001-10-01" @default.
• W2137671011 modified "2023-09-30" @default.
• W2137671011 title "Solution Structure, Hydrodynamics and Thermodynamics of the UvrB C-terminal Domain" @default.
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• W2137671011 doi "https://doi.org/10.1080/07391102.2001.10506734" @default.
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