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By Nelson D.L., Cox M.M.

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Additional resources for Solutions Manual for Lehninger Principles of Biochemistry 5ed. (Freeman, 2008)

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What does this analysis tell you about the identity of the protein? (b) Try using different portions of the amino acid sequence. Do you always get the same result? (c) A variety of websites provide information about the three-dimensional structure of proteins. org) or SCOP. (d) In the course of your Web searches, what did you learn about the cellular function of the protein? ” Paste the first 30 amino acid residues of the sequence into the search box and submit the sequence for comparison. The table that returns includes many proteins that have 100% sequence identity with these 30 residues.

2608T_ch03sm_S26-S43 2/1/08 11:45AM Page 31 ntt 102:WHQY028:Solutions Manual:Ch-03: Chapter 3 Amino Acids, Peptides, and Proteins (c) COOϪ ϩ COOϪ ϩ COOϪ COOϪ ϩ ϩ H3N C H H3N C H H C NH3 H C NH3 H C CH3 H 3C C H H C CH3 H3C C H CH2 CH2 CH2 CH2 CH3 CH3 CH3 CH3 7. 69, corresponding to the ionization of the carboxyl and the protonated amino groups, respectively. The titration of di-, tri-, and larger oligopeptides of alanine also shows the ionization of only two functional groups, although the experimental pKa values are different.

What pI would you predict for the pepsin proteins? What functional groups must be present to confer this pI on pepsin? Which amino acids in the proteins would contribute such groups? Answer Pepsin proteins have a relatively low pI (near the pH of gastric juice) in order to remain soluble and thus functional in the stomach. ) As pH increases, pepsins acquire a net charge and undergo ionic interactions with oppositely charged molecules (such as dissolved salts), causing the pepsin proteins to precipitate.

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