Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model

@article{Perutz1968ThreedimensionalFS,
  title={Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model},
  author={M. Perutz and H. Muirhead and J. M. Cox and L. Goaman},
  journal={Nature},
  year={1968},
  volume={219},
  pages={131-139}
}
The secondary structure of the haemoglobin chains is similar to that of myoglobin, but some of the helical segments are more irregular and some parts of the non-helical segments have different conformations. The structure of the contacts between unlike subunits suggests that the tetramer, rather than the αβ dimer, is the functional unit of haemoglobin. 
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References

SHOWING 1-10 OF 23 REFERENCES
The structure of haemoglobin. IX. A three-dimensional Fourier synthesis at 5.5 Å resolution: description of the structure
  • 74
Chemical modification of hemoglobins: a study of conformation restraint by internal bridging.
  • S. Simon, W. Konigsberg
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1966
  • 25
  • PDF
On the mechanism of the dissociation of haemoglobin.
  • 196
...
1
2
3
...