| Literature DB >> 6331541 |
T Jue, G N La Mar, K Han, Y Yamamoto.
Abstract
1H NMR spectroscopy has been used to measure the proximal histidyl labile ring proton (NH) rates of exchange with bulk solvent in the individual subunits of hemoglobin (Hb) A. These protons displayed a substantial decrease in their exchange rates in comparison with related monomeric proteins and exhibited sensitivity to the quarternary state. With the beta subunit NH, the exchange behaviour was similar to an allosterically responsive subset of protons, which have been identified using 1H-3H methods (Englander, J.J., R. Rogero, and S. W. Englander, 1983, J. Mol. Biol. 169:325-344). Assuming similar exchange mechanisms for the two subunits, the NMR data suggested a more flexible alpha than beta subunit in Hb A.Entities:
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Year: 1984 PMID: 6331541 PMCID: PMC1434941 DOI: 10.1016/S0006-3495(84)84004-7
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033