Bioinformatic scaling of allosteric interactions in biomedical isozymes

J.C. Phillips

Physica A: Statistical Mechanics and its Applications, 2016, vol. 457, issue C, 289-294

Abstract: Allosteric (long-range) interactions can be surprisingly strong in proteins of biomedical interest. Here we use bioinformatic scaling to connect prior results on nonsteroidal anti-inflammatory drugs to promising new drugs that inhibit cancer cell metabolism. Many parallel features are apparent, which explain how even one amino acid mutation, remote from active sites, can alter medical results. The enzyme twins involved are cyclooxygenase (aspirin) and isocitrate dehydrogenase (IDH). The IDH results are accurate to 1% and are overdetermined by adjusting a single bioinformatic scaling parameter. It appears that the final stage in optimizing protein functionality may involve leveling of the hydrophobic limits of the arms of conformational hydrophilic hinges.

Keywords: Self-organized criticality; Scaling; Bioinformatic; Allosteric; Amino acid; Sequence (search for similar items in EconPapers)
Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:457:y:2016:i:c:p:289-294

DOI: 10.1016/j.physa.2016.03.038

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