3.Fill the data in the following table: What in Concentration of Amino Acids: 4. Prepare a graph of your results, ploting mL of NaOH versus pH. Plot cach of the two utrations (not the dry run) using standard graph paper or Excel. Remember to label the graph axes and provide enough tick marks along each axis to be useful. It is casy to forget these steps when using roftware; write the information in by hand, if necessary. 5. From a titration curve it is easy to discem the inflection point ( (l) ). This is the point when 1 equivalent of base has been added. In this experiment you use 10mL of 0.1M amino acid or 1 millimole of amino acid (fully protonated). As stated in the introduction, the completely protonated amino acid can donate two protons during the titration. It will take one equivalent ( 1 millimole) of base to titrate the first proton (on the acid group) and another equivalent to titrate the second proton (on the amine group). Find the pl and label it on each graph. Note- An equivalent refers to the moles of OH or H+added with each addition of NaOH. It is determined by multiplying the volume of NaOH added by the concentration of the NaOH. 6. Since the pK Kcid is the midpoint on the first leg. you can find the pK Kwad at 0.5 equivalents of base. Likewise, the pKKmi can be found at 1.5 equivalents of base. Find and label the pKn and pKamia for each graph (if possible)