Abstract
A characterization of how biomolecules interact combined with a knowledge of their concentration, distribution, environment, and regulation of synthesis is required to understand how biological systems work. The characterization of molecular interactions involves demonstration of binding, identification of binding sites and estimation of quantitative parameters such as binding strength, rate constants, and binding stoichiometry. Equilibrium binding constants are informative regarding the physiological importance of a given acceptor-ligand interaction and various methods (TABLE 1) have been devised for the measurement of this parameter. All methods listed may allow for determination of binding constants but some are more widely applicable than others. The ideal method should be applicable to a wide range of interacting biomolecules under physiological conditions using low amounts of native material at high precision and speed. Of the methods listed in TABLE 1 only mass spectrometry (MS) and capillary electrophoresis (CE) are in principle applicable for the study of native and not necessarily purified biomolecules using minute amounts of material. However, the analytical conditions in the two methods are quite different and none of the methods can be said to be generally applicable even though there are now many examples of the uses of MS (this book) and CE (TABLE 2) for the measurement of various biospecific interactions.
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Heegaard, N.H.H. (1998). Biospecific Interactions Measured by Capillary Electrophoresis. In: Ens, W., Standing, K.G., Chernushevich, I.V. (eds) New Methods for the Study of Biomolecular Complexes. NATO ASI Series, vol 510. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9046-4_24
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DOI: https://doi.org/10.1007/978-94-015-9046-4_24
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