Functional roles of natural products: The involvement of extended arrays of weak interactions in cooperative binding phenomena. Williams, D., Searle, M., Groves, P., Mackay, J., Westwell, M., Beauregard, D., & Cristofaro, M. Pure and Applied Chemistry, 66(10-11):1975-1982, 1994. doi abstract bibtex A factorisation of the free energy of binding into various “costs” and “benefits” has provided the basis for a semi-quantitation of some weak interactions in solution. It has become clear that the entropie cost of motional restriction on binding (A + B → A.B) increases with increasing exothermicity of the association; this exothermicity must of course reflect not only interactions at the interface between A and B, but also the change in bonding throughout B (if B represents the receptor). We illustrate cooperativity and anti-cooperativity by reference to effects of ligand binding (as models of classical agonists and antagonists) on the dimerisation of vancomycin-group antibiotics. Since dimerization of receptors (promoted by ligand binding) is a common theme in biological signalling, it must presumably have an advantage in natural selection. We suggest that concurrent demands of ligand binding and receptor dimerization may permit a more specific control of those ligand structures which can cause signal transmission. In this way, specificity in biological signalling might be aided. © 1994 IUPAC
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title = {Functional roles of natural products: The involvement of extended arrays of weak interactions in cooperative binding phenomena},
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year = {1994},
pages = {1975-1982},
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abstract = {A factorisation of the free energy of binding into various “costs” and “benefits” has provided the basis for a semi-quantitation of some weak interactions in solution. It has become clear that the entropie cost of motional restriction on binding (A + B → A.B) increases with increasing exothermicity of the association; this exothermicity must of course reflect not only interactions at the interface between A and B, but also the change in bonding throughout B (if B represents the receptor). We illustrate cooperativity and anti-cooperativity by reference to effects of ligand binding (as models of classical agonists and antagonists) on the dimerisation of vancomycin-group antibiotics. Since dimerization of receptors (promoted by ligand binding) is a common theme in biological signalling, it must presumably have an advantage in natural selection. We suggest that concurrent demands of ligand binding and receptor dimerization may permit a more specific control of those ligand structures which can cause signal transmission. In this way, specificity in biological signalling might be aided. © 1994 IUPAC},
bibtype = {article},
author = {Williams, D.H. and Searle, M.S. and Groves, P. and Mackay, J.P. and Westwell, M.S. and Beauregard, D.A. and Cristofaro, M.F.},
doi = {10.1351/pac199466101975},
journal = {Pure and Applied Chemistry},
number = {10-11}
}
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