Direct measurement of equilibrium constants for high-affinity hemoglobins.

@article{Kundu2003DirectMO,
  title={Direct measurement of equilibrium constants for high-affinity hemoglobins.},
  author={Suman Kundu and Scott A. Premer and Julie A. Hoy and James T. Trent and Mark S Hargrove},
  journal={Biophysical journal},
  year={2003},
  volume={84 6},
  pages={3931-40}
}
The biological functions of heme proteins are linked to their rate and affinity constants for ligand binding. Kinetic experiments are commonly used to measure equilibrium constants for traditional hemoglobins comprised of pentacoordinate ligand binding sites and simple bimolecular reaction schemes. However, kinetic methods do not always yield reliable equilibrium constants with more complex hemoglobins for which reaction mechanisms are not clearly understood. Furthermore, even where reaction… CONTINUE READING

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