Opossum hemoglobin. The amino acid sequences of the alpha and beta chains.

@article{Stenzel1979OpossumHT,
  title={Opossum hemoglobin. The amino acid sequences of the alpha and beta chains.},
  author={Peter Stenzel and Bernadine Brimhall and R. T. Jones and John A. Black and Anne McLachlan and D R Gibson},
  journal={The Journal of biological chemistry},
  year={1979},
  volume={254 6},
  pages={
          2071-6
        }
}
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Using an Escherichia coli gene expression system, human hemoglobin mutants are engineered having the distal histidine and valine residues replaced by other amino acids, finding that the steric bulk of thedistal residues is not the primary determinant of the Fe-CO ligand vibrational frequencies.
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TLDR
The infrared spectra for carbon monoxide complexed to hemoglobins were examined in the C-O stretch region and provide qualitative and quantitative information on the structural dynamics, stability, and ligand binding properties of hemoglOBins.
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TLDR
It is argued that continuing studies of marsupial and monotreme globins, particularly molecular studies on gene organisation and regulation, are likely to contribute significantly to the understanding of gene and organismal evolution.
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