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.
Allosteric proteins : lessons to be learned from the hemoglobin intermediates / M. Perrella, R. Russo. - In: NEWS IN PHYSIOLOGICAL SCIENCES. - ISSN 0886-1714. - 18:6(2003 Dec), pp. 232-236. [10.1152/nips.01451.2003]
Allosteric proteins : lessons to be learned from the hemoglobin intermediates
M. PerrellaPrimo
;R. RussoUltimo
2003
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.
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