Adair binding function

COOPERATIVITY ALLOSTERISM INDUCED FIT MODEL MONOD-WYMAN-CHANGEUX MODEL INDEPENDENT BINDING LINKED FUNCTIONS ADAIR EQUATION POSITIVE COOPERATIVITY NEGATIVE COOPERATIVITY KOSMOTROPES CHAOTROPIC AGENTS HOFMEISTER SERIES Kp, Kq, K .. . ... 

The shape of the saturation curve defined by Eq. (9.59) depends on the values of L and c. If L = 0, then the T form of the protein does not exist and Y = XR[X]/(1 + XR[X]). This defines a hyperbolic binding function. Similarly if L = Y = XT[X]/(1 + XT[X]). Thus, deviations from hyperbolic binding occur only if both R and T forms exist otherwise the situation described for the Adair equation in Example 9.13 applies since binding is independent and identical at each site. 

Here, the equalities in parentheses are strictly valid whenever the sites are identical in the strict sense. Otherwise, one should interpret these intrinsic binding constants as average quantities, as discussed in Appendix J. Since Eq. (6.8.5) has the correct functional form of 8(P), it is easy to obtain a good fit of the experimental data with the four Adair constants A, t = 1,2, 3,4. 

Linked-function mechanisms for cooperative binding interaction of metabolites and/or drugs, based on the presence of two or more different conformational states of the protein or receptor. See Adair Equation Cooperative Ligand Binding Hemoglobin Hill Equation Plot Koshland-Nemethy-Filmer Model Monod-Wyman-Changeux Model Negative Cooperativity Positive Cooperativity... 

This expression is called a linked function and indicates how the binding of ligands at nearby sites can influence each other. See also Basic Regulatory Kinetics Cooper-ativity Allosterism Feedback Effectors Bohr Effect Hemoglobin Le Chatelier s Principle Adair Equation... 

Fig. 1.2. Fractions of molecules of hemoglobin occupied by a different number of oxygen molecules (m f.) as a function of the fraction of occupied oxygen binding sites in hemoglobin. Curves are calculated by using parameters of the Adair equation given in Fig. 1.1.

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