Cooperative binding model

Cooperative binding model. NPA atomic charges were calculated at the MP2/... 

Figure 6.2. Proposed model for quinolone-DNA cooperative binding in the inhibition of DNA gyrase [32], (Reprinted with permission American Chemical Society.)...

The indirect correlation is the major source of cooperativity in biochemical systems, such as hemoglobin (Chapter 6) or allosteric enzymes (Chapter 8). The model treated in this section is the simplest binding model having indirect correlation. We now examine some of the outstanding properties of the indirect correlation... 

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... 

The symmetry model (fig. 2.4) of allostery can describe the cooperative binding of substrate to enzyme (homotropic effect), as well as the influence of effector molecules on the activity of enzymes (heterotropic effect). 

Biochemists now know a great deal about the T and R states of hemoglobin, but much remains to be learned about how the T —> R transition occurs. Two models for the cooperative binding of ligands to proteins with multiple binding sites have greatly influenced thinking about this problem. 

Fig. 5-15a). The concerted model assumes that the subunits of a cooperatively binding protein are functionally identical, that each subunit can exist in (at... 

Two major models have been proposed to explain the cooperative binding of ligands to multisubunit proteins the concerted model and the sequential model. 

Table 10.2 Equilibria, binding constants, extended site binding model parameters and cooperativity for the formation of the Eu(III) complex of 10.9 (L).

The cooperative binding of O2 by hemoglobin and the allosteric effects in many enzymes require interaction between sites that are widely separated in space. The MWC model was proposed in 1965 to incorporate allosteric and conformational effects in an explanation of enzyme cooperativity. The seminal observation was that most cooperative proteins have several identical subunits (protomers) in each molecule (oligomer) this situation is imperative for binding cooperativity. The MWC model is defined as follows ... 

Using the model applied earlier for the description of the helix-coil transition in DNA molecules104 the parameter of cooperativity a was calculated105 for the PAA-PDMAEM reaction and was found to be near value for the helix-coil transition. This indicates the resemblance of the processes based on cooperative binding of macromolecules of weak synthetic polyelectrolytes and cooperative transition in DNA molecules. 

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