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Binding size dependence

The binding of the antibody is size-dependent. Only the preincubation of the antibodies with oligopectates of degree of polymerization (DP) > 9 inhibits the binding to pectin immobilized in the wells of an ELISA test (Fig. 9.a, b). The difference between dimerized DPS and DP9 oligomers lies in the fact that dimerized DP9 could accommodate five calcium ions between their two chains whereas DPS could only four, which is apparently insufficient for the complexes to resist thermal agitation. [Pg.141]

Krueger S, Vent S, Roesch N. 1997. Size dependence of bond length and binding energy in palladium and gold clusters. Ber Bunsenges Phys Chem 101 1640-1643. [Pg.559]

Vesicle size was found to affect reaction kinetics for the alkaline hydrolysis and thiolysis of p-nitrophenyl octanoate, with small vesicles being more effective as catalysts, and it was concluded that this size dependence itself was brought about by differences in ion dissociation, substrate binding constants, and intrinsic reactiv-... [Pg.29]

It was found that the catalytic reactivity and the substrate binding profile depend upon the size and the generation of the dendrons. Since the reactions obey Michaelis-Menten kinetics, this family of catalysts was given the name dendrizyme , alluding to enzymes. The dendrizyme/substrate binding constant... [Pg.226]

Avoid introducing air bubbles. Slowly pour slurry down a thin glass rod inserted into empty column. The column and bed sizes depend on the amount of His-tagged protein to be purified. Generally, the binding capacity of Ni-NTA superflow is 5-10 mg protein per mL resin Ni-NTA superflow is supplied as 50% slurry. [Pg.103]

The volume of distribution of a peptide or protein drug is determined largely by its physico-chemical properties (e. g., charge, lipophilicity), protein binding, and dependency on active transport processes. Due to their large size - and therefore limited mobility through biomembranes - most therapeutic proteins have small volumes of distribution, typically limited to the volumes of the extracellular space [26, 51]. [Pg.28]

T. Ohgi and D. Fujita, Consistent Size Dependency of Core-Level Binding Energy Shifts and Single-Electron Tunneling Effects in Supported Gold Nanoclusters, Phys. Rev. B 66, 115410-115415 (2002). [Pg.58]

Figure 10.5 shows the size dependence of the coordination number of noble gases at the two binding sites, which is calculated at the concentration of 0.001 M. At the substrate binding site, the coordination number becomes exponentially larger as the size of gas increases (Fig. 10.5a). At the internal site, the coordination number becomes larger with increase in the gas size up to a k, 3.4 A, while it decreases in the region where a > 3.4 A (Fig. 10.5b). As a result, argon has the largest binding affinity to the internal site. These results demonstrate that the 3D-RISM theory has the ability to describe ligand-size... Figure 10.5 shows the size dependence of the coordination number of noble gases at the two binding sites, which is calculated at the concentration of 0.001 M. At the substrate binding site, the coordination number becomes exponentially larger as the size of gas increases (Fig. 10.5a). At the internal site, the coordination number becomes larger with increase in the gas size up to a k, 3.4 A, while it decreases in the region where a > 3.4 A (Fig. 10.5b). As a result, argon has the largest binding affinity to the internal site. These results demonstrate that the 3D-RISM theory has the ability to describe ligand-size...

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