Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability.

@article{Karantza1995ThermodynamicSO,
  title={Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability.},
  author={V Karantza and Alexandros Baxevanis and Ernesto Freire and Evangelos N. Moudrianakis},
  journal={Biochemistry},
  year={1995},
  volume={34 17},
  pages={
          5988-96
        }
}
The thermal stability of the core histone dimer H2A-H2B has been studied by high-sensitivity differential scanning calorimetry and circular dichroism spectroscopy. The unfolding transition temperature of the 28 kDa H2A-H2B dimer increases as a function of both the ionic strength of the solvent and the total protein concentration. At neutral pH and physiological ionic strength, the thermal denaturation is centered at about 50 degrees C with a corresponding enthalpy change of about 40 kcal/mol of… CONTINUE READING
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