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Allosteric (long-range) interactions can be surprisingly strong in proteinsof biomedical interest. Here we use bioinformatic scaling to connect priorresults on nonsteroidal anti-inflammatory drugs to promising new drugs thatinhibit cancer cell metabolism. Many parallel features are apparent, whichexplain how even one amino acid mutation, remote from active sites, can altermedical results. The enzyme twins involved are cyclooxygenase (aspirin) andisocitrate dehydrogenase (IDH). The IDH results are accurate to 1% and areoverdetermined by adjusting a single bioinformatic scaling parameter. Itappears that the final stage in optimizing protein functionality may involveleveling of the hydrophobic cutoffs of the arms of conformational hydrophilichinges.

Bioinformatic Scaling of Allosteric Interactions in Biomedical Isozymes