In this experiment, appose you forget to mark the position of the solvent front

Question

In this experiment, appose you forget to mark the position of the solvent front when you tested the hydrolystae of aspartame against the other amino acids. Is it still possible to determine how many amino acids were present in the hydrolysate? Explain Could you still identify what those amino acids were? Explain your answer. What can you not do? There are polarity and molecular weight differences between aspartic acid and phenylalanine: Aspartic acid has a polar, acidic side chain and a smaller molecular weight; phenylalanine has a nonpolar side chain and a larger molecular weight Based on the R_f values you obtained for these two amino acids in the solvent employed, which amino acid migrated faster and which of these two properties influenced the rate of migration?

Explanation / Answer

a. Yes, it is possible to determine the number of amino acids present in the hydrolysate. Aspartame is a methyl ester of the two amino acids (dipeptide) aspartic acid/phenylalanine. Aspartic acid and phenylalanine have different polarity so they travel different distances in the given solvent system. The Rf value of phenyl alanine is larger than the aspartic acid. So, based on this property you can distinguish the two amino acids, though you have not labelled.

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