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  1. Starting from a fully protonated state, the pK a 's of the acidic functions range from 1.8 to 2.4 for -CO 2 H, and 8.8 to 9.7 for -NH 3(+). The isoelectric points range from 5.5 to 6.2. Titration curves show the neutralization of these acids by added base, and the change in pH during the titration.

  2. AMINO ACID TITRATION. Objectives. To study the titration curves of amino acid. To determine the pKa values. To determine isoelectric point (pI). To determine buffering regions. Amino acid general formula and classification. Amino acids consist of: a basic amino group ( —NH2 ) . an acidic carboxyl group ( —COOH) a hydrogen atom ( —H)

  3. Chemicals. Acetic acid 98% R, Formic acid, anhydrous R. Titrant. c(HClO 4) = 0.1 mol/L. Weigh a sample of 0.24 to 0.25 g Aspartame, accurately to 0.1 mg, in a titration beaker. Pipette 1.5 mL of anhydrous formic acid into the beaker and dissolve the sample. Finally add 50 mL of acetic acid 98%.

  4. A summary of the important curves. The way you normally carry out a titration involves adding the acid to the alkali. Here are reduced versions of the graphs described above so that you can see them all together. More complicated titration curves. Adding hydrochloric acid to sodium carbonate solution

  5. Our calculations yielded the total fraction of aspartic acids expected to be protonated at pHs 0 through 8 in increments of 1 with an overall titration curve centered close to the nominal ASP...

  6. Anionic form. The ionic form of the amino acid present in an aqueous solution depends on the pH of the solution. In this experiment, you will identify an unknown amino acid through acid-base titration. Titration curves of amino acids are very useful for identification.

  7. Titration curves of ASP residues by secondary structure. The native pK a for aspartic acid is indicated.

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