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- W2503708093 abstract "The classic description of the quaternary structure change accompanying cooperative ligand binding by hemoglobin (Hb) assumes the existence of two stable tetrameric, quaternary structural classes: the fully-oxygenated (R-state) and the completely deoxygenated (T-state) structures. To characterize the structures that actually occur in solution, to improve the ability of the NMR experiment to distinguish members within a structural class, and ultimately to use this improved ability to assign the structures of intermediate ligation states to members within such families, we have been developing a new approach in which experimental pseudocontact shifts are analyzed to obtain a site-specific description of structural changes produced by mutations in the intradimer interface." @default.
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- W2503708093 date "2003-07-23" @default.
- W2503708093 modified "2023-10-11" @default.
- W2503708093 title "An Approach to NMR Treatment of Structural Perturbations in Paramagnetic Proteins too Big for Solution Structure Determination" @default.
- W2503708093 doi "https://doi.org/10.1021/bk-2003-0858.ch012" @default.
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