Unique capabilities are offered by NMR spectroscopy for probing specific interactions of enzymes with substrates and substrate analogues, for characterizing the multiple conformations of the complexes, and for measuring rates of a wide range of dynamic processes. The most extensive studies of this type have been directed at complexes formed by dihydrofolate reductase with antifolate drugs and are described in this review.
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J. Feeney (2000) studied this question.