Abstract
The specificity of the interaction of biopolymers with one another and with small molecules in binding and catalysis is based primarily on the fit of complementary structures. When this is inadequate to generate the high fidelity required in the replication and synthesis of DNA and proteins, specificity is enhanced by editing or proofreading mechanisms. These add kinetic control of product formation. The magnitudes of the interaction energies of groups in proteins with each other and of nucleotide pairing may be measured from simple kinetic experiments with enzymes. The energies thus estimated are far higher than those expected from experiments on simple models.
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