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human hemoglobin a chains in monocarboxylated state
Global fold of the human hemoglobin a chains in monocarboxylated state. Using standard 2D NMR methods we assigned resonances for more than 70% of the residues in these chains [1], and also in b-chains [2] and the whole tetramer [3]. A diamagnetic model of the unliganded state of a-chains was obtained by replacing the heme iron by the Zn2+ ion [4]. The side chains in the figure indicate the localization of the largest perturbations induced by the ligand binding.
1. Martineau, L. and C. Craescu, T., Sequential assignment of the proton NMR spectrum of isolated a(CO) chains from human adult hemoglobin. European Journal of Biochemistry, 1992, 205: p. 661-670.
2. Craescu, C., T. and J. Mispelter, Assignment of proton resonances in the NMR spectrum of carbonmonoxy b subunit tetramers. European Journal of Biochemistry, 1988, 176: p. 171-178.
3. Craescu, C., T., J. Mispelter, and Y. Blouquit, Coupling of tertiary and quaternary changes in human hemoglobin: a 1D and 2D NMR study of hemoglobin Saint Mandé (bN102Y). Biochemistry, 1990, 29: p. 3953-3958.
4. Martineau, L. and C. Craescu, T., Sequential assignment of proton resonances in the NMR spectrum of Zn-substituted a chains from human hemoglobin. European Journal of Biochemistry, 1993, 214: p. 383-393.