Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry.

@article{Henzl2009CharacterizationOP,
  title={Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry.},
  author={Michael T. Henzl},
  journal={Methods in enzymology},
  year={2009},
  volume={455},
  pages={259-97}
}
The elucidation of structure-affinity relationships in EF-hand proteins requires a reliable assay of divalent ion affinity. In principle, isothermal titration calorimetry (ITC) should be capable of furnishing estimates for Ca2+- and Mg2+-binding constants in these systems. And because the method yields the binding enthalpy directly, ITC can provide a more… CONTINUE READING