Notes on usage of the Kinetics tutorial
|| The Java program above has three panels.
- The top depicts a graph of the Enzyme rate vs. [S]. There are two lines on the first graph here:
- The black one is a reference graph whose Data (Km and Vmax) ALWAYS remain unchanged even as the scale on the graph changes.
- The RED one is the one whose data that you manipulate with the sliders.
- A relative scale of the graph is indicated at the top.
- The two bar graphs on the top right represent formation about the current conditions chosen
- The panel at top right gives a bar graph representation of the current [S], [P], and enzyme rates as well as
- the log of the final equilibrium position.
- The middle panel provides numerical representation of the same data.
- units for the parameters
- all concentrations ([S], [P], [E]) are in M/l (Molar)
- kcat = sec-1
- enzyme rates (vmax and vo=Rate of [P]) = moles/sec (moles of product produced per sec)
- Km = Molar
- kcat/Km = Molar sec
- Keq is unitless
- The bottom panel provides some interaction.
- Sliders on the bottom panel allow you to independently alter the [S], [P], [E], kcat, Km, Vmax, kcat/Km, Keq and the Hill coefficient independently to observe the effects.
- The Radio buttons on the right allow you to maintain the [P]= 0 or allow [P] to accumulate.
In the latter case you should observe that eventually the ratio of [S] and [P] will come to the same ratio as indicated in the "final equilibrium position" window. This final equilibrium position can be altered by changing the DG of the reaction.
| The bar graphs update in at a rate 10 times faster than "real time" this is solely to make the changes in the graph visible and more interesting to watch.
| Alter each parameter one at a time. Observe what the changes are in values that are linked as well as what happens to the graph itself.|
| Notes: the kcat/Km, kcat, Km, Vmax and [E] values are linked computationally observe what happens to each as you alter any of the one of the set.