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Explain the Equilibrium Dialysis?
Equilibrium dialysis is a useful technique for studying the binding of a small uncharged solute species (a ligand) to a macromolecule. The macromolecule solution is placed on one side of a membrane through which it cannot pass, with a solution without the macro- molecule on the other side, and the ligand is allowed to come to transfer equilibrium across the membrane. If the same solute standard state is used for the ligand in both solutions, at equilibrium the unbound ligand must have the same activity in both solutions. Measure- ments of the total ligand molality in the macromolecule solution and the ligand molality in the other solution, combined with estimated values of the unbound ligand activity coefficients, allow the amount of ligand bound per macromolecule to be calculated.
If a codon is CDC, what proportion of nucleotide changes in the third position result in a new amino acid? If the codon is AGG, what proportion of changes in the first position res
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