Published July 1, 1972
| public
Journal Article
Open
Observation of cooperative ionizations in hemoglobin
- Creators
- Huestis, Wray H.
- Raftery, Michael A.
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.
Additional Information
© 1972 by the National Academy of Sciences. Communicated by Jerome Vinograd, May 8, 1972. We thank D.L. Huestis for assistance in calculation of titration curves for interacting ionizations. This work was supported by a National Science Foundation Predoctoral Fellowship to W.H. Huestis, by USPHS Grants GM 16424 and GM 14452, and by a National Institutes of Health Career Development Award (GM 46414) to M.A. Raftery. Contribution No. 4447 from the Church Laboratory of Chemical Biology.Files
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Additional details
- Eprint ID
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- Resolver ID
- CaltechAUTHORS:HUEpnas72
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2008-02-27Created from EPrint's datestamp field
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2019-10-03Created from EPrint's last_modified field