Cooperativity, absolute interaction, and algebraic optimization

We consider a measure of cooperativity based on the minimal interaction required to generate an observed titration behavior. We describe the corresponding algebraic optimization problem and show how it can be solved using the nonlinear algebra tool SCIP. Moreover, we compute the minimal interactions and minimal molecules for several binding polynomials that describe the oxygen binding of various hemoglobins under different conditions. We compare their minimal interaction with the maximal slope of the Hill plot, and discuss similarities and discrepancies with a view towards the shapes of the binding curves.

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Bibliographic Details
Main Authors: Kaihnsa, N., Ren, Y., Safey El Din, M., Martini, J.W.R.
Format: Article biblioteca
Language:English
Published: Springer 2020
Subjects:AGRICULTURAL SCIENCES AND BIOTECHNOLOGY, OPTIMIZATION METHODS, SYSTEMS, COMPONENTS, MATHEMATICAL MODELS, COMPUTER APPLICATIONS, OXYGEN, HAEMOGLOBIN,
Online Access:https://hdl.handle.net/10883/21019
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Description
Summary:We consider a measure of cooperativity based on the minimal interaction required to generate an observed titration behavior. We describe the corresponding algebraic optimization problem and show how it can be solved using the nonlinear algebra tool SCIP. Moreover, we compute the minimal interactions and minimal molecules for several binding polynomials that describe the oxygen binding of various hemoglobins under different conditions. We compare their minimal interaction with the maximal slope of the Hill plot, and discuss similarities and discrepancies with a view towards the shapes of the binding curves.