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TITRATION CURVES
A typical strong acid-strong base titration curve is shown in Figure 1 below. In this lab
you will be titrating weak acids which look a bit different, but still have the steep section
in the middle. In previous titration experiments you have determined the equivalence
point of the titration by observing the color change of an indicator. When using a pH
meter to monitor the titration, the endpoint is determined by the inflection point of the
curve. This provides a more accurate determination of the equivalence point. The
inflection point is the steepest part of the curve, and is also the point on the curve where
the curvature changes. In calculus terms, this is the point where the second derivative
equals zero.
The LoggerPro program that you will be using to collect the data has a feature which will
allow you to calculate and plot the second derivative of pH as a function of volume of
base added. There is a video you can watch which goes over how to make this plot and
find the endpoint.
In this lab you will work with a partner to complete two titrations. First you will titrate a
weak acid (KHP) with a ~0.1 M sodium hydroxide solution. From the results of this
titration you will be able to calculate the exact concentration of the NaOH. (In other
words, you will standardize the NaOH. Do you remember why this is necessary?) Next
you will titrate an unknown polyprotic acid. From your titration data, you will be able to
calculate the acid ionization constants and the molecular weight of the unknown acid.
A pH meter will be used to measure the pH. So that you can monitor each titration in real
time, you will enter and plot the data on a computer as the titration proceeds.
Directions
1. Set up a titration apparatus as shown below. Position the pH electrode in the
solution and adjust its position so that it is not struck by the stirring bar.
4. Set up a buret with the NaOH solution provided. Fill to the 0.00 mL line.
5. You will be given a vial containing KHP. Dissolve the entire sample in about 40
mL of water and determine the exact mass by weighing the vial before and after.
6. Add a few drops of phenolphthalein to the acid. This is not necessary because you
will be finding the equivalence point from the graph, but it is useful to observe
how the equivalence point you get from the graph compares to what you would
determine using the indicator.
7. In your notebook, calculate the expected endpoint based on the mass of KHP
used.
8. Record the initial pH of the acid solution. This is the pH with no NaOH added.
You will be entering data manually as you titrate. Record the initial volume (0.00
mL) of NaOH in the buret. As you continue to enter data, the titration curve will
be displayed on the screen.
10. For each addition of base, record the exact volume of NaOH added and the exact
pH. Remember that burets should be read to the hundredths place. Note: When
the pH begins to change rapidly you will need to add base in much smaller
increments in order to produce a change of only 0.2 units.
11. Record the volume of base and the pH at the point when the solution turns pink.
You do not need this information for your calculations, but it will be interesting to
observe how or if the two methods for determining the equivalence point differ.
12. Continue titrating to beyond the equivalence point, where the curve begins to
flatten out.
13. Add a column to your data table to calculate the second derivative of the data and
plot this data to determine the equivalence point. Review the posted video for how
to do this. Save the file to your ACS account or to a removable drive. Do not save
to the hard drive or your data will be lost.
14. Repeat the steps above with your sample of an unknown polyprotic acid. Record
the unknown number. Remember that you will have two equivalence points. If
you add base too quickly, you may miss the first one.
Before completing your post lab you must submit your results to the Google Form for
checking.