Abstract
The relationship between the binding function Y and the state function R of an oligomeric protein has been analysed for the general two-state allosteric model. It is shown that this relation is determined by the numerical values of the inherent parameters of the model. The shape of the function Y = f ( R) can therefore be strictly concave, strictly convex or inverse sigmoidal according to the conditions. In the two-state allosteric model only a dimeric protein can display a linear relationship between Y and R . In the paper general criteria for the estimation of the state function R from experimentally obtained conformational parameters are discussed.
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