Performance tradeoffs are ubiquitous in biology (and an essential feature of HOT).
Well-studied examples include biomechanics
(strength vs. speed), animal behavior (fight vs. flight), and, until recently, enzymes (stability vs. activity).
The patterns of stability and activity among naturally-occurring, homologous enzymes have traditionally been attributed to
flexibility tradeoffs. However, flexibility is sufficiently complex that it cannot mediate generic tradeoffs
outside the active site. Furthermore, enzymes with unnatural combinations of
high stability and high activity can be created in the laboratory. These enzymes are exceptionally rare among all
possible amino acid sequences, suggesting that evolutionary, not physicochemical, mechanisms are responsible for the
stability-activity patterns among natural homologs. Check out these slides for more information.
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