The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms.

@article{Tame1996TheCS,
  title={The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms.},
  author={Jeremy R.H. Tame and Jennifer C. Wilson and Roy E Weber},
  journal={Journal of molecular biology},
  year={1996},
  volume={259 4},
  pages={749-60}
}
We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic… CONTINUE READING

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