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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 10 (1998), S. 14-23 
    ISSN: 0899-0042
    Keywords: biological signalling ; ristocetin A ; cooperativity ; dimerization ; asymmetry ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The self-regulation of biological signalling receptors via homodimerization is discussed in relation to the symmetry changes occurring when these receptors bind their target ligand. The idea of positive and negative cooperativity between dimerization and ligand binding, mediated by changes in the symmetry of the system, as a source of signalling control is considered; and an analogy made with the homodimerization of a glycopeptide antibiotic, ristocetin A, which displays negative cooperativity. Finally, the regulation of the bacterial aspartate receptor and the human growth hormone receptor is discussed as a function of ligand-induced asymmetry. Chirality 10:14-23, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-9023
    Keywords: cooperativity ; drug design ; hydrophobic effect ; non-covalent interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The reliable estimation of binding constants by computational means for drugs binding to receptors represents one of the major challenges in molecular recognition. Many approaches to this problem have relied on the partitioning of binding free energy according to each of the interactions which are made or broken on binding, e.g., hydrogen bonds, salt bridges, π-π interactions, or the hydrophobic effect. With particular reference to the hydrophobic effect, we illustrate how such partitioning ignores one of the fundamental properties of systems of non-covalent interactions, namely that of cooperativity. This leads to estimates for the free energy benefit of the hydrophobic effect which vary according to the method of determination used, and whether the system in which the measurements are taken exhibits cooperativity. The context dependence of the magnitude of the hydrophobic effect illustrates the problem associated with considering weak interactions in isolation from the system in which they occur. The approach of partitioning binding affinities can be very useful, but until the problem of cooperativity can be better addressed by computational chemists, there remains the possibility that attempts to estimate at least some binding constants will unfortunately be seriously flawed.
    Type of Medium: Electronic Resource
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