The 1.8 A structure of carbonmonoxy-beta 4 hemoglobin. Analysis of a homotetramer with the R quaternary structure of liganded alpha 2 beta 2 hemoglobin.

@article{Borgstahl1994The1A,
  title={The 1.8 A structure of carbonmonoxy-beta 4 hemoglobin. Analysis of a homotetramer with the R quaternary structure of liganded alpha 2 beta 2 hemoglobin.},
  author={Gloria E O Borgstahl and Paul H Rogers and Arthur Arnone},
  journal={Journal of molecular biology},
  year={1994},
  volume={236 3},
  pages={817-30}
}
The beta-chains isolated from the human hemoglobin alpha 2 beta 2 heterotetramer self-assemble to form a beta 4 homotetramer. We report the structure of the carbonmonoxy-beta 4 (CO beta 4) tetramer refined at a resolution of 1.8 A. Compared to the three known quaternary structures of human hemoglobin, the T state, the R state and the R2 state, the quaternary structure of CO beta 4 most closely resembles the R state. While the degree of structural similarity between CO beta 4 and the R state of… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.

Similar Papers

Loading similar papers…