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SUMMARY:Experiments for Enzyme Kinetic Models - Atkinson\, A (MD Anderson 
 Cancer Center)
DTSTART:20110815T104500Z
DTEND:20110815T113000Z
UID:TALK32356@talks.cam.ac.uk
CONTACT:Mustapha Amrani
DESCRIPTION:Enzymes are biological catalysts that act on substrates. The s
 peed of reaction as a function of substrate concentration typically follow
 s the nonlinear Michaelis-Menten model. The reactions can be modified by t
 he presence of inhibitors\, which can act by several different mechanisms\
 , leading to a variety of models\, all also nonlinear. \n\nThe talk will d
 escribe the models and derive optimum experimental designs for model build
 ing. When the model is known these include D-optimum designs for all the p
 arameters for which we obtain analytical solutions. Ds-optimum designs for
  the inhibition constant are also of scientific importance. \n\nWhen the m
 odel is not known\, the choice is often between two three-parameter models
 . These can be combined in a single four-parameter model. Ds-optimum desig
 ns for the parameter of combination provide a means of establishing which 
 model is true. However\, T-optimum designs for departures from the individ
 ual models provide tests of maximum power for departures from the models. 
 With two models on an equal footing\, compound T-optimum designs are requi
 red. Their properties are compared with those of the Ds-optimum designs in
  the combined model\, which have the advantage of being easier to compute.
  \n
LOCATION:Seminar Room 1\, Newton Institute
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