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Cooperative binding effect

Dendrimer-saccharide conjugates are unique nanodevices in their ability to tightly bind lectins and other proteins with specific saccharide recognition capabilities [174], The multivalency of dendrimer surfaces allows for a cooperative binding effect. Where single saccharide-receptor interactions are relatively weak, the multiplicity of poly(valent) interactions introduced by conjugating a... [Pg.423]

Figure 8. Schematic drawing of cooperative effect (a) independent binding (b) cooperative binding. Figure 8. Schematic drawing of cooperative effect (a) independent binding (b) cooperative binding.
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). [Pg.92]

Hughes, M. P., Smith, B. D., Enhanced carboxylate binding using urea and amide-based receptors with internal Lewis acid coordination A cooperative polarization effect. J. Org. Chem. 1997, 62, 4492—4499. [Pg.317]

Figures 5.11A and B show the characteristic sigmoid curves obtained as a result of interaction between the substrate site, the stimulating modulator site, and the inhibitory modulator site for K and M classes of enzymes. The curves in the absence of modulators are homotropic effects caused by cooperative binding of the substrate. Heterotropic modulators, which can be either positive or negative in their actions, are molecules other than the substrate. Figures 5.11A and B show the characteristic sigmoid curves obtained as a result of interaction between the substrate site, the stimulating modulator site, and the inhibitory modulator site for K and M classes of enzymes. The curves in the absence of modulators are homotropic effects caused by cooperative binding of the substrate. Heterotropic modulators, which can be either positive or negative in their actions, are molecules other than the substrate.
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 ... [Pg.270]

Ligand-induced conformational changes in the protein can result in both cooperative and antagonistic binding effects on other ligands binding to the same protein. An example of a cooperative interaction is the enhancement of the interactions of progesterone and testosterone with human serum albumin (HSA) by the palmitate ion. [Pg.1027]


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