Theory of the measurement of weak molecular complexes. I. General considerations

Deranleau, David A.

doi:10.1021/ja01043a004

Cited by 391 publications

(203 citation statements)

References 3 publications

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“…However, because a double reciprocal plot gives too much weight to the initial, least-precise points in a titration (18), it was used only for establishing nH after So.5 and AE were determined by using the saturation binding curve. These parameters (So., and nH) define both equilibrium constants, K1 and K2.…”

Section: Methodsmentioning

confidence: 99%

Effect of interchain disulfide bond on hapten binding properties of light chain dimer of protein 315.

Zidovetski¹,

Licht²,

Pecht³

1979

Proc. Natl. Acad. Sci. U.S.A.

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The hapten binding characteristics of the covalent light chain dimer, derived from the murine IgA secreted by plasmacytoma MOPC-315, to two nitroaromatic compounds, epsilon-N-(2,4-dinitrophenyl)-L-lysine and 4-(alpha-N-alanine)-m-nitrobenz-2-oxa-1,3-diazole, were investigated by differential spectroscopic titrations. The binding curves for both haptens were found to display sigmoidity similar to that reported earlier for the reduced and alkylated dimer held together by noncovalent bonds only. However, the presence of the interchain disulfide bond in the covalent dimer was found to cause marked changes in its binding properties. The data, like those obtained for the noncovalent dimer, fit the allosteric model of Monod, Wyman, and Changeux in which binding of the first hapten to the dimer causes a conversion of both sites of the protein molecule from a lower to a higher affinity conformation. However, the binding parameters show that both the affinity and the positive cooperativity in the interaction between haptens and the covalent dimer are significantly enhanced. The differences in the parameters of the binding and of the allosteric transition caused by the presence of the interchain disulfide bond demonstrate the existence of longitudinal interactions in immunoglobulin derivatives. These properties of the light chain dimer make it a potential model for the receptors present on thymus-derived lymphocytes.

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Section: Methodsmentioning

confidence: 99%

Effect of interchain disulfide bond on hapten binding properties of light chain dimer of protein 315.

Zidovetski¹,

Licht²,

Pecht³

1979

Proc. Natl. Acad. Sci. U.S.A.

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“…It is well known that even under ideal conditions there is considerable error associated with the calculation of equilibrium constants (113)(114)(115)(116)(117)(118). To illustrate, we contrast the porphyrin/viologen case with the simplest case involving two hypothetical absorbing species 2) The spectra of each of the two viologen-associated H 2 TCPp 4 -complexes were shifted by only a few nanometers to the red of the monomer porphyrin spectrum ( Figure 23); therefore, the three components were not spectroscopically well resolved.…”

Section: Determination Of Association Constantsmentioning

confidence: 99%

“…Association constants are most accurate when the equilibrium concentration is equal to the lowest concentration species (116,117,119). Coulombic repulsion should make the forward reaction highly strategy for calculating equilibrium constants…”

Section: Determination Of Association Constantsmentioning

confidence: 99%

“…This is particularly true when the associations are weak (117), as is observed in porphyrin/viologen complexation. Thus, data uncertainty must be minimized in order to obtain meaningful values for the association constants (119).…”

mentioning

confidence: 91%

“…Association constants are difficult to determine mathematically when multicomponent equilibria are observed (113)(114)(115)(116)(117)(118)(119)(120). This is particularly true when the associations are weak (117), as is observed in porphyrin/viologen complexation.…”

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confidence: 99%

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The Effect of Two Viologens on the Solution Speciation of Tetrakis([rho]-carboxyphenyl)porphine

Clarke¹

2000

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Synthesis, Conformation, and Binding Properties of Cyclodextrin Homo- and Heterodimers Connected through Their Secondary Sides

et al. 1998

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The synthesis of homo-and heterocyclodextrin (CD) dimers, containing two CD moieties that are linked through their secondary sides by aliphatic or 2,2'-bipyridyl spacers is described. In these dimers, the glucose units to which the spacers are linked have been transformed into altrose units. The dimers with an octamethylene spacer show self-complexation of the spacer in one of the CD moieties in aqueous solution, as revealed by 1 H and 13 C NMR spectroscopy. Using high-resolution (600 and 800 MHz) NMR spectroscopy and a variety of 2D NMR techniques, an assignment of nearly all of the 1 H NMR signals of two of the CD dimers was made, affording detailed information about the structure of these compounds in water. The self-inclusion of the spacers leads to lower binding affinities for ditopic guest molecules like p-toluidino-6-naphthalene sulfonate (TNS) derivatives and porphyrins. When a rigid 2,2'-bipyridyl group is used to connect the two CD moieties, self-inclusion of the spacer is not possible. This results in the formation of different complexes with ditopic guest molecules, for example, a 2:2 complex with a porphyrin. The CD heterodimers described in this paper contain an a-CD and a b-CD moiety. These dimers display site-specific binding of guest molecules.

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Theory of the measurement of weak molecular complexes. I. General considerations

Cited by 391 publications

References 3 publications

Effect of interchain disulfide bond on hapten binding properties of light chain dimer of protein 315.

Effect of interchain disulfide bond on hapten binding properties of light chain dimer of protein 315.

The Effect of Two Viologens on the Solution Speciation of Tetrakis([rho]-carboxyphenyl)porphine

Synthesis, Conformation, and Binding Properties of Cyclodextrin Homo- and Heterodimers Connected through Their Secondary Sides

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