Asymmetric Cooperativity in a Symmetric Tetramer: Human Hemoglobin*

@article{Ackers2006AsymmetricCI,
  title={Asymmetric Cooperativity in a Symmetric Tetramer: Human Hemoglobin*},
  author={G. K. Ackers and J. Holt},
  journal={Journal of Biological Chemistry},
  year={2006},
  volume={281},
  pages={11441 - 11443}
}
A longstanding challenge in macromolecular biochemistry has been the question of how the four "active site" hemes of human hemoglobin (Hb) interact cooperatively over widely separated intramolecular distances (i.e. 24 -37 A) to regulate the O 2 affinity of the molecule. In the modern era of Hb research, beginning with the availability of crystal structures for both the deoxy and fully ligated tetramers by the late 1960s, the problem of subunit-subunit communication has been addressed by… Expand
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Tertiary and quaternary allostery in tetrameric hemoglobin from Scapharca inaequivalvis.
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The Hill coefficient: inadequate resolution of cooperativity in human hemoglobin.
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Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.
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