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Exercise 21.2 Cooperative Binding Consider the binding of ligand (substrate, drug) A to a macromolecule M which is a cyclic a tetramer (square). The states

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Exercise 21.2 Cooperative Binding Consider the binding of ligand (substrate, drug) A to a macromolecule M which is a cyclic a tetramer (square). The states of the minding complex are symbolized through a binary string, where M is denoted 0000, and MA, is denoted 1111. There exists nearest-neighbor coopera- tivity defined by the parameter such that (1100) [1001] (1010] [1010 and the scaled substrate concentration is defined as usual (1000) (0000) A. Tabulate the statistical weights of all species relative to that of the unbound state as a function of and s. B. Derive an expression for the average number of sites occupied per macromolecule as a function of and s. C. Plotting and Visualization Plot the normalized coverage of the macromolecule as a function of substrate concentration for several values of 7 including T = 1. You may wish to scale the abscissa as was done in Figure 21.3.2, but that is up to you. Exercise 21.2 Cooperative Binding Consider the binding of ligand (substrate, drug) A to a macromolecule M which is a cyclic a tetramer (square). The states of the minding complex are symbolized through a binary string, where M is denoted 0000, and MA, is denoted 1111. There exists nearest-neighbor coopera- tivity defined by the parameter such that (1100) [1001] (1010] [1010 and the scaled substrate concentration is defined as usual (1000) (0000) A. Tabulate the statistical weights of all species relative to that of the unbound state as a function of and s. B. Derive an expression for the average number of sites occupied per macromolecule as a function of and s. C. Plotting and Visualization Plot the normalized coverage of the macromolecule as a function of substrate concentration for several values of 7 including T = 1. You may wish to scale the abscissa as was done in Figure 21.3.2, but that is up to you

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