Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism.

@article{Gelin1983HemoglobinTS,
  title={Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism.},
  author={Bruce R. Gelin and Angel W-M Lee and Martin Karplus},
  journal={Journal of molecular biology},
  year={1983},
  volume={171 4},
  pages={489-559}
}
Analysis of the tertiary structural alterations in hemoglobin induced by ligand binding demonstrates that an allosteric core composed of the heme, histidine F8, the FG corner and part of the F-helix plays an essential role in co-operativity. This conclusion is based on structural and spectroscopic data and theoretical studies of hemoglobin chains. The methodology employed in the calculations is presented with details of the empirical energy function. Energy minimized structures of the… CONTINUE READING

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