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. 1976 Nov;73(11):3793–3797. doi: 10.1073/pnas.73.11.3793

Role of subunit interfaces in the allosteric mechanism of hemoglobin.

C Chothia, S Wodak, J Janin
PMCID: PMC431212  PMID: 1069263

Abstract

We calculate the surface area buried in subunit interfaces of human deoxyhemoglobin and of horse methemoglobin. A larger surface area is buried in deoxy- than in methemoglobin as a result of tertiary and quaternary structure changes. In both molecules the dimer-dimer interface is closepacked. This implies that hydrophobicity stabilizes the deoxystructure, the free energy spent in keeping the subunits in a low-affinity conformation being compensated by hydrophobic free energy due to the smaller surface area accessible to solvent.

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Selected References

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