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From a biochemical context, considering the following two dissociation reactions and their respective dissociation constants for a protein-ligand complex:
P*A + B ⇔ P + A + B, this contains the a dissociation constant called Ka = 4 x 10^-3 M
P*B + A ⇔ P + A + B, this contains the a dissociation constant called Kb = 2 x 10^-7 M
Compare the values of Ka and Kb; Does the free protein bind ligand A or ligand B more tightly? I know that a lower dissociation value means tighter bonding or "higher affinity," so the free protein should bind to ligand B more tightly, but can someone explain to me why this is the case?
P*A + B ⇔ P + A + B, this contains the a dissociation constant called Ka = 4 x 10^-3 M
P*B + A ⇔ P + A + B, this contains the a dissociation constant called Kb = 2 x 10^-7 M
Compare the values of Ka and Kb; Does the free protein bind ligand A or ligand B more tightly? I know that a lower dissociation value means tighter bonding or "higher affinity," so the free protein should bind to ligand B more tightly, but can someone explain to me why this is the case?