Sigmoidicity in allosteric models (Q794948)

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Sigmoidicity in allosteric models
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    Sigmoidicity in allosteric models (English)
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    1983
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    For the saturation function, the state function as well as for the steady-state rate function of the Monod-Wyman-Changeux allosteric model analytical conditions of sigmoidicity are derived. They are shown as regions of sigmoidicity in a parameter space constituted by the allosteric constant parameter and the nonexclusive binding coefficient for each ligand. In the first two cases the number of the interacting protomers, in the third the ratio of turnover of the T and R states play the role of share parameters. In the Koshland-Nemethy-Filmer allosteric model state and saturation functions are identical. The sigmoidicity in that case depends only on the degree of coupling between subunits and on the relative stability of the asymmetrically induced subunit interactions. The feature of sigmoidicity is important because it stands necessarily for positive cooperativity in allosteric models. With respect to modelling sigmoidicity constitutes a criterion which may be used to discriminate between the current allosteric models by direct comparison, for a given ligand, of the state and saturation functions or by qualitative comparison of the saturation function for several ligands.
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    regulation of enzymatic activities
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    saturation function
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    state function
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    steady-state rate function
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    Monod-Wyman-Changeux allosteric model
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    analytical conditions of sigmoidicity
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    regions of sigmoidicity
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    Koshland- Nemethy-Filmer allosteric model
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    cooperativity
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