Abstract
In principle, any technique that separates bound from unbound ligand, or occupied from unoccupied protein, can be used to monitor binding. As a general rule, highest accuracy is achieved when the concentration of the protein in binding studies is approximately equal to K d (within about one order of magnitude either way), this makes it easier to determine the concentration difference between bound and total ligand. Since the supply of protein is usually a limiting factor in research, binding studies are expensive and the sample size must be reduced as much as possible. Considerable progress has been made in this direction over the years.
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Buxbaum, E. (2011). General Conditions for Interpretable Results. In: Biophysical Chemistry of Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7251-4_41
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DOI: https://doi.org/10.1007/978-1-4419-7251-4_41
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