Free energy changes and components implicit in the MWC allosteric model for the cooperative oxygen binding of hemoglobin.

Abstract

Hill's plots of oxygen binding isotherms reveal the presence of a transition between two different oxygen affinities at the beginning and end of the isotherm. They correspond to the two conformations anticipated by the MWC model, namely, the T and R conformations at the beginning and end of oxygen binding, when the lower affinity of the T form develops into… (More)
DOI: 10.1021/bi400319c

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Cite this paper

@article{Bucci2013FreeEC, title={Free energy changes and components implicit in the MWC allosteric model for the cooperative oxygen binding of hemoglobin.}, author={Enrico M. Bucci and Stefania Pucciarelli and Mauro Angeletti}, journal={Biochemistry}, year={2013}, volume={52 24}, pages={4149-56} }