Direct measurement of protein binding energetics by isothermal titration calorimetry.

@article{Leavitt2001DirectMO,
  title={Direct measurement of protein binding energetics by isothermal titration calorimetry.},
  author={Stephanie A. Leavitt and Ernesto Freire},
  journal={Current opinion in structural biology},
  year={2001},
  volume={11 5},
  pages={560-6}
}
Of all the techniques that are currently available to measure binding, isothermal titration calorimetry is the only one capable of measuring not only the magnitude of the binding affinity but also the magnitude of the two thermodynamic terms that define the binding affinity: the enthalpy (AH) and entropy (AS) changes. Recent advances in instrumentation have facilitated the development of experimental designs that permit the direct measurement of arbitrarily high binding affinities, the coupling… CONTINUE READING

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