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Analysing molecular recognition and binding

Now that we have covered the main theoretical models of binding and molecular recognition events, including their analytical equations and equilibrium binding constants, we must show that equilibrium binding constants can be derived from the experimental equivalents of B and [L]. [Pg.348]

From this, the corresponding value of B may be determined according to the following relationship  [Pg.349]

Provided that values of B are then determined under identical experimental conditions but with different values of mL , an accurate binding isotherm will be generated that obeys [Pg.349]

Isothermal titration calorimetry (ITC) is almost the ultimate titration methodology in that this technique is based entirely upon titration of heat energy and then deconvolution of this information into equilibrium binding constant information. However, the real beauty of this technique is that it engages directly with the thermodynamics of receptor-ligand binding interactions. [Pg.352]

Every species i in aqueous solution is credited with a chemical potential At, (aq) at a given concentration c, that is defined according to [Pg.352]


The molecular recognition of septanose carbohydrates has been investigated in depth by using concanavalin A68 as a model lectin. Complex formation was analysed by STD experiments and showed the first direct evidence of binding, by a natural protein, for this class of ring-expanded carbohydrate molecules. [Pg.343]

The x-ray stmcture of complexes of TcAChE with HA and other AChE inhibitors displayed that these noncovalent inhibitors vary greatly in their stmctures and bind to different sites of the enzyme, offering many different starting points for future dmg design. To rationalize the stmcmral requirements of AChE inhibitors, Kaur and Zhang attempted to derive a coherent AChE-inhibitor recognition pattern based on literature data of molecular modeling and quantitative SAR analyses. [Pg.167]

We have already explored the reasons why K, and Kj values are the primary data obtained in our analyses—that is, to gain insight into weak binding forces. Molecular recognition events can be quite potent— bind ing interactions of tens of kcal / mol are common—and the consequences in a biological context or in a designed sensor can be quite dramatic. However, when we try to analyze the physical underpiimings of an event—the stock-in-trade of... [Pg.222]


See other pages where Analysing molecular recognition and binding is mentioned: [Pg.348]    [Pg.349]    [Pg.351]    [Pg.353]    [Pg.355]    [Pg.357]    [Pg.359]    [Pg.361]    [Pg.363]    [Pg.348]    [Pg.349]    [Pg.351]    [Pg.353]    [Pg.355]    [Pg.357]    [Pg.359]    [Pg.361]    [Pg.363]    [Pg.159]    [Pg.126]    [Pg.517]    [Pg.337]    [Pg.68]    [Pg.123]    [Pg.586]    [Pg.44]    [Pg.123]    [Pg.126]    [Pg.42]    [Pg.68]    [Pg.123]    [Pg.145]    [Pg.151]    [Pg.156]    [Pg.246]    [Pg.132]    [Pg.423]    [Pg.237]    [Pg.515]    [Pg.159]    [Pg.525]    [Pg.219]    [Pg.222]    [Pg.399]    [Pg.419]    [Pg.2238]    [Pg.523]    [Pg.536]    [Pg.262]    [Pg.48]    [Pg.126]    [Pg.61]    [Pg.28]    [Pg.32]    [Pg.368]   


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Molecular recognition

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Molecular recognition and binding

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