The INI has a new website!

This is a legacy webpage. Please visit the new site to ensure you are seeing up to date information.

Skip to content



Experiments for Enzyme Kinetic Models

Atkinson, A
Monday 15 August 2011, 11:45-12:30

Seminar Room 1, Newton Institute


Enzymes are biological catalysts that act on substrates. The speed of reaction as a function of substrate concentration typically follows the nonlinear Michaelis-Menten model. The reactions can be modified by the presence of inhibitors, which can act by several different mechanisms, leading to a variety of models, all also nonlinear.

The talk will describe the models and derive optimum experimental designs for model building. When the model is known these include D-optimum designs for all the parameters for which we obtain analytical solutions. Ds-optimum designs for the inhibition constant are also of scientific importance.

When the model is not known, the choice is often between two three-parameter models. These can be combined in a single four-parameter model. Ds-optimum designs for the parameter of combination provide a means of establishing which model is true. However, T-optimum designs for departures from the individual models provide tests of maximum power for departures from the models. With two models on an equal footing, compound T-optimum designs are required. Their properties are compared with those of the Ds-optimum designs in the combined model, which have the advantage of being easier to compute.


[pdf ]


The video for this talk should appear here if JavaScript is enabled.
If it doesn't, something may have gone wrong with our embedded player.
We'll get it fixed as soon as possible.

Back to top ∧