One must understand that amino acids all have special characteristics and properties. For instance, each amino acid has a unique molecular weight value and this driven on its molecular structure contents such as its carboxyl and amine structures and its linked pKa values.
In order to determine whether our provided …show more content…
We took note that both of the titration sessions were essentially identical, save for a few instructed weights. For both titration sessions, we weighed an approximate amount of amino acid—the first time, we were instructed to acquire about 0.8 grams of glycine, the second time, we were instructed to acquire about 0.5 grams of unknown amino acid. I was able to acquire 0.810 grams and 0.53 grams, respectively. We, then, dissolved the amino acid into 50 mL of deionized water. During this time, we also calibrated our pH meter and recorded its pH readings for water after calibration. These values were 4.68 and 5.88, respectively. Right after, we began reading the pH of our amino acid (the first one was 5.17 and the second session was 3.55). We then proceeded by adding 25 mL of 0.5 M of HCl. The pH values after this addition are 1.56 and 1.34. We filled a cleansed biuret with 0.5 M NaOH solution. The main process begins with us closely monitoring changes in pH as we added NaOH from the biuret at 0.5 mL increments. We refilled the biuret with NaOH when it neared empty. We halted the titration process when both the pH stabilized and we reached a pH level range of 12-13. All data collected was graphed to visually view the