Crystallographic studies on manganese hemoglobin.
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Chemical Phenomena↗
Biomedical subjects
K Moffat
Publications and source records attributed to K Moffat.
Gelation of sickle cell hemoglobin: effects of hybrid tetramer formation in hemoglobin mixtures.
The altered gelation behavior found in mixtures of sickle cell hemoglobin with other hemoglobins is due to the formation of hybrid hemoglobin tetramers from unlike dimers. The hemoglobins need not possess the deoxy quaternary structure for gelation to occur; liganded forms are also capable of participation in gelation.
Chemical Phenomena↗
The ligand-binding properties of desHis (146beta) hemoglobin.
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Amino Acid Sequence↗
Covalent inhibitors of cooperativity in hemoglobin.
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Animals↗
Structure-function relationships in hemoglobins: scientific aspects.
Both proximal and distal molecular processes which could contribute to lowered ligand affinity, and hence to cooperativity, have been identified from a comparison of macromolecular structures; most have been successfully modelled by ingenious model heme derivatives. More work is needed to decide which of these processes are operative at each stage of the ligand binding process, which is both kinetically and structurally complex.
Binding Sites↗