| answer 1:5 - Correct! Let's proceed to the analysis of the residuals for simple binding to a monomeric protein. The residuals look very good because they randomly and cross the zero line at high frequency, suggesting that the fit has a no systematic errors.       In this tutorial some important concepts have been presented, namely: 1) The C50, free concentration of the ligand require to saturate half the available binding sites. The C50 is always a function of the equilibrium dissociation constant Kd; in a simple monomeric protein this relationship assumes its simplest possible form: C50 = Kd. 2) The procedure of normalization of the signal, which allows one to obtain the fraction of liganded sites [PX] / [P]tot. This tutorial is complete. Back to table of content |
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