title: Allosteric proteins: lessons to be learned from the hemoglobin intermediates.
abstract: Allosteric proteins, such as hemoglobin, are assemblies of functional units, which undergo quaternary structural transitions in response to concentration changes of a specific ligand. Functional properties of hemoglobin ligation intermediates indicate that the tertiary structural changes induced by the ligand do not promote an equilibrium of quaternary structures.
authors: Dipartimento di Scienze e Tecnologie Biomediche, Università di Milano, I-20090 Segrate (MI), Italy.
authors: Michele
authors: M
authors: Perrella
authors: Rosaria
authors: R
authors: Russo
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008954:Models, Biological; D015394:Molecular Structure
chemical_list: D006454:Hemoglobins; D008024:Ligands