Why is the first dissociation constant larger than the second?
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The smaller the dissociation constant, the more tightly bound the ligand is, or the higher the affinity between ligand and protein. For example, a ligand with a nanomolar (nM) dissociation constant binds more tightly to a particular protein than a ligand with a micromolar (μM) dissociation constant.
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Explanation:
For polyprotic acids, the first Ka is always the largest, followed by the second, etc.; this indicates that the protons become successively less acidic as they are lost.
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