Binding experiments

Vacancy Formation Energy (eV) Element Tight-Binding Experiment Fixed Relaxed... 

Minimal criteria and optimal conditions for binding experiments ... 

For optimum binding experiments, the following conditions should... 

Binding experiments are done in three general modes saturation, displacement, and kinetic binding. 

Effect of excess receptor in binding experiments saturation binding curve (4.6.9)... 

Effect of Excess Receptor in Binding Experiments Saturation Binding Carve... 

Binding experiments can yield direct measurements of ligand affinity (Chapter 4). However, with the use of null techniques these same estimates can also be obtained in functional studies. The concepts and procedures used to do this differ for partial and full agonists. 

Another frequent question asked considers whether the mean of a value measured by two separate methods differs significantly. For example, does the mean pKB value of an antagonist measured in a binding experiment differ significantly from its affinity as an antagonist of agonist function The value of t for the comparison of the mean values xml and xm2 can be calculated with the following equation ... 

Analysis of Ligand Binding in the Intact Cell. A model of LR dynamics in the intact cell consistent with the results of these studies is presented in Figure 6, and a fit to the data of a polarization binding experiment is shown. The model has these characteristics ... 

Binding assays for the saxitoxins were conducted with homogenized rabbit brain and saxitoxin exchange-labelled with tritium at C-11 (92, 93). If the various saxitoxins were available with suitably intense radiolabels, then the equilibrium dissociation constant, K, could be measured directly for each. Since only saxitoxin is currently available with the necessary label, the binding experiments instead measure the ability of a compound to compete with radiolabelled saxitoxin for the binding site. The value obtained, Kj, corresponds to the uilibrium dissociation constant, K, that would be observed for the compound if it were measured directly. Affinity is defined for this assay as the reciprocal of Kj. The affinities of several of the saxitoxins (94) are summarized in Figure 11, expressed relative to saxitoxin and plotted on a logarithmic scale. 

The interaction of neurotoxins with the Na channel are usually studied using electrophysiological experiments, Na uptake experiments, and also binding experiments involving radiolabelled toxins. 

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