The measurement of accurate chemical equilibria is vitally important for understanding recognition of a substrate by an enzyme or receptor. While experimental methods measuring binding equilibria are relatively straight forward, the precise analysis of data is often in error. Simplifying or inappropriate graphing techniques lead to incorrect equilibrium constant definitions. As the free energy of binding may also be estimated from equilibrium constants, inaccuracies in measurements affect both kinetic and thermodynamic analyses. This seminar will showcase the benefits of using visual aids, available with dynamic computer simulation, to display equilibrium binding curves under a variety of conditions. One-step and multi-step binding schemes will be covered, leading up to understanding cooperative binding of substrates by a dimeric enzyme. The computer simulation software, KinTek Explorer, allows for observation of all enzyme and substrate species and the direct manipulation of equilibrium constants; thus, it is a highly beneficial tool in teaching and understanding chemical equilibria. Also, instead of using simplifying equations to define cooperativity, KinTek Explorer inputs all steps that affect substrate binding, leading to a more accurate approach to equilibrium analysis. In the free student version of KinTek Explorer, synthetic data can be generated from a model and subsequently fit by students, which can provide a viable substitute for laboratory exercises at any undergraduate institution. Various levels of difficulty may be designed for different undergraduate courses, from binding equilibrium analyzed for a one-step model, to four-step linked equilibria as observed with the oxygen-binding properties of hemoglobin.<br/>

Teaching principles of chemical equilibria using computer simulation methods

256th National Meeting (2018)

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