Molecular symmetry of the dodecamer subunit of Lumbricus terrestris hemoglobin.

@article{Martin1996MolecularSO,
  title={Molecular symmetry of the dodecamer subunit of Lumbricus terrestris hemoglobin.},
  author={Philip D. Martin and Klaus Eisele and Mary Agnes Doyle and Alexei Kuchumov and Daniel A. Walz and E G Arutyunyan and Serge N. Vinogradov and Brian F P Edwards},
  journal={Journal of molecular biology},
  year={1996},
  volume={255 1},
  pages={170-5}
}
The principal functional subunit of the approximately 3500 kDa extracellular Lumbricus terrestris hemoglobin is a 213 kDa dodecamer of four chemically distinct globin chains, consisting of a non-covalent complex of three trimer submits (disulfide-bonded chains a, b and c) and three monomer subunits (chain d). X-ray diffraction of crystals of the dodecamer grown at neutral pH, were found to be monoclinic, with the unit cell dimensions: a = 112.3 A, b = 190.0 A, c = 69.6 A, beta = 102.0 degrees… CONTINUE READING

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