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. 1991 May 15;88(10):4472–4475. doi: 10.1073/pnas.88.10.4472

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

W A Eaton 1, E R Henry 1, J Hofrichter 1
PMCID: PMC51682  PMID: 2034685

Abstract

The transition state for the R in equilibrium with T quaternary conformational change of hemoglobin has thermodynamic properties much closer to those of the R conformation than to those of the T conformation. This finding is based on a comparison of activation and equilibrium enthalpy and entropy changes and on the observation of a linear free energy relationship between quaternary rate and equilibrium constants. A previous theoretical study [Janin, J. & Wodak, S. J. (1985) Biopolymers 24, 509-526], using a highly simplified energy function, suggests that the R-like transition state is the result of a reaction pathway with the maximum buried surface area between alpha beta dimers.

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Selected References

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