1. Consider the peptides P-A-I-G-E and M-A-T-T. a. Draw the structure of each peptide at a pH of 7.0 b. Draw the structure of each peptide at a pH of 12.0 c. Calculate the pl. of both peptides. Based on your answer, do you think these two peptides can be separated using ion exchange chromatography at a pH of 5? Explain.

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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1. Consider the peptides P-A-I-G-E and M-A-T-T.
a. Draw the structure of each peptide at a pH of 7.0
b. Draw the structure of each peptide at a pH of 12.0
c. Calculate the pl of both peptides. Based on your answer, do you think these two
peptides can be separated using ion exchange chromatography at a pH of 5?
Explain.
Transcribed Image Text:1. Consider the peptides P-A-I-G-E and M-A-T-T. a. Draw the structure of each peptide at a pH of 7.0 b. Draw the structure of each peptide at a pH of 12.0 c. Calculate the pl of both peptides. Based on your answer, do you think these two peptides can be separated using ion exchange chromatography at a pH of 5? Explain.
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Introduction

Formation of the peptide bond neutralises any charge due to the alpha-amino group and alpha-carboxyl group, therefore the net charge on a peptide or protein is due to the ionisation of the amino acid residue side group. Some amino acids have positively charged side groups while some have negatively charged side groups. This makes protein amphoteric which at a particular pH can have a net positive charge or negative charge, except at isoelectric pH where the net charge is zero. 

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