Association constant interaction

Schematically, response is produced by the full agonist ([AR]) complex—which interacts with the stimulus response system with equilibrium association constant Ke—and the partial agonist (lower efficacy), which interacts with an equilibrium association constant K ...

AR] complex) interacts with an equilibrium association constant Ke (to yield an efficacy term x) and the allosterically altered agonist-bound receptor complex ([ABR] complex) interacts with the cell with equilibrium association constant K e (to yield an altered efficacy x7). It is useful to define a ratio of efficacies for the native and allosterically modulated receptor of x /x (denoted , where = x//x). 

The receptor can bind both the probe (agonist, radioligand, [A]) and allosteric modulator ([B]). The agonist (7.11) bound receptor signal through the normal operational model ([AR] complex interacting with cellular stimulus-response machinery with association constant Ke) and in a possibly different manner when the allosteric modulator is bound (complex [ABR] interacting with cell with... 

The commonly used method for the determination of association constants is by conductivity measurements on symmetrical electrolytes at low salt concentrations. The evaluation may advantageously be based on the low-concentration chemical model (lcCM), which is a Hamiltonian model at the McMillan-Mayer level including short-range nonelectrostatic interactions of cations and anions [89]. It is a feature of the lcCM that the association constants do not depend on the physical... 

In Eq. (15) 2 qB/r is the coulombic part of the mean force potential, and Wjj is the noncoulombic part. The earlier association constants of Fuoss, Prue, and Bjerrum are special cases of this general chemical model [15]. The importance of noncoulombic interactions is proved [ 16] by ... 

In contrast, reaction of ligand 72 with 4,4 -biphenyldiboronic acid has been successful and diboronate 73 is obtained in yields of 33%. This complex acts as a receptor for the paraquat dication forming a 1 1 complex with an association constant of 320 in acetone. The intermolecular forces responsible for the complexation are ion-dipole stabilization between the dative N B dipoles and the two cationic centers in paraquat, attractive tz-tz interactions between... 

A case similar to the slow, practically irreversible inhibition of jack bean a-D-mannosidase by swainsonine is represented by the interaction of castanospermine with isomaltase and rat-intestinal sucrase. Whereas the association constants for the formation of the enzyme-inhibitor complex were similar to those of other slow-binding glycosidase inhibitors (6.5 10 and 0.3 10 M s for sucrase and isomaltase, respectively), the dissociation constant of the enzyme-inhibitor complex was extremely low (3.6 10 s for sucrase) or could not be measured at all (isomaltase), resulting in a virtually irreversible inhibition. Danzin and Ehrhard discussed the strong binding of castanospermine in terms of the similarity of the protonated inhibitor to a D-glucosyl oxocarbenium ion transition-state, but were unable to give an explanation for the extremely slow dissociation of the enzyme-inhibitor complex. 

Mattel et al., this book). The three variant enzymes were still able to interact and bind to PGIP with association constants comparable to that of the wild type enzyme. 

The kinetic parameters of each interaction are reported in Table 1. These data show that the values of the equilibrium association constant Ka for the interaction of PGIP with the different yeast-e ressed polygalacturonases do not differ significant, but in each case they are 2 5 times lower wlien conq)ared to that of the F. moniliforme i2yme. This is probably... 

Significantly, it has been shown that coordination of nucleobases can enhance base pairing interactions (115). These findings confirm previous theoretical calculations (116). The association constant for Watson-Crick interactions between 9-EtG and 1-MeC was 6.9 M 1, determined... 

The aniline-zinc porphyrin interaction has also been exploited to form dimers. Hunter (60) reported the dimerization of porphyrins functionalized at one meso position with ortho or meta aniline groups (47, 48, Fig. 15). Both compounds showed concentration-dependent H NMR spectra with large upfield shifts for the aniline protons. The dimerization constants are 160 and 1080 M-1 respectively for 47 and 48, and these values are an order of magnitude higher than the association constants of simple reference complexes (K — 10 and 130 M 1 respectively), which is indicative of cooperative self-assembly. The complexa-tion-induced changes in chemical shift were used to obtain three-dimensional structures of the dimers. 

Macrocyclic receptors made up of two, four or six zinc porphyrins covalently connected have been used as hosts for di- and tetrapyridyl porphyrins, and the association constants are in the range 105-106 M-1, reflecting the cooperative multipoint interactions (84-86). These host-guest complexes have well-defined structures, like Lindsey s wheel and spoke architecture (70, Fig. 27a), and have been used to study energy and electron transfer between the chromophores. A similar host-guest complex (71, Fig. 27b) was reported by Slone and Hupp (87), but in this case the host was itself a supramolecular structure. Four 5,15-dipyridyl zinc porphyrins coordinated to four rhenium complexes form the walls of a macrocyclic molecular square. This host binds meso-tetrapyridyl and 5,15-dipyridyl porphyrins with association constants of 4 x 107 M-1 and 3 x 106 M-1 respectively. 

Honda, S., Taga, A., Suzuki, K., Suzuki, S., and Kakehi, K., Determination of the association constant of monovalent mode protein-sugar interaction by capillary zone electrophoresis, /. Chromatogr., 597, 377, 1992. 

The noncovalent binding of a series of oxo-squaraine dyes 9a-e to BSA was evaluated by measurement of absorption, emission, and circular dichroism [63]. The magnitude of the association constants (Ks) for the dye-BSA complexes depended on the nature of the side chains and ranged from 34 x 103 to 1 x 107 M-1. Depending on the side chains, the Ks increase in the order [R1 = R2 = butyl-phthalimide] < R1 = R2 = cetyl] <[RJ = R2 = ethyl] <<[R = butyl-phthalimide, R2 = butyl-sulfonate] <<[RJ = R2 = butyl-sulfonate]. These dyes seem to interact mainly with a hydrophobic cavity on BSA. However, the association constants Ks increase substantially when the side chains are selected from butyl sulfonate. 

In principle, in both slow and fast exchange limits, the analysis of the ligand-protein interaction could be performed by a direct integration of the two well-separated resonances of free and bound ligand and by the analysis of their chemical shift. However, these methods are limited by the broadness of the protein-ligand NMR spectra, and numerical values of association constants are barely obtainable. 

Equilibrium association constants for interaction of mouse eIF4E (28—217) with various cap analogs at 20°. The final KAS value for each cap analog was calculated as a weighted average of independent titrations. 

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