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. 1972 Jul;69(7):1887–1891. doi: 10.1073/pnas.69.7.1887

Observation of Cooperative Ionizations in Hemoglobin

Wray H Huestis 1, Michael A Raftery 1
PMCID: PMC426825  PMID: 4505667

Abstract

19F-Nuclear magnetic resonance studies of specifically fluorinated hemoglobin derivatives have been used to determine the apparent pKa of the histidine β146 imidazole in deoxyhemoglobin. The titration of this residue was found to be abnormally sharp, particularly in the presence of diphosphoglyceric acid. The explanation advanced for this unusual titration curve may have implications for the mechanism of cooperative ligand binding. The possible role of such ionizations is discussed in light of some chemical evidence that the cooperative binding process is governed to a greater extent by internal nonpolar forces than by electrostatic interactions of exposed groups.

Keywords: 19F-NMR, specifically labeled proteins, molecular regulation mechanisms, hydrophobic interactions

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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