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We consider a measure of cooperativity based on the minimal absoluteinteraction required to generate an observed titration behavior. We describethe corresponding algebraic optimization problem and show how it can be solvedusing the nonlinear algebra tool \texttt{SCIP}. Moreover, we compute theminimal absolute interactions for various binding polynomials that describe theoxygen binding of various hemoglobins under different conditions. Whilecalculated minimal absolute interactions are consistent with the expectedoutcome of the chemical modifications, it ranks the cooperativity of themolecules differently than the maximal Hill slope.

Cooperativity, Absolute Interaction, and Algebraic Optimization