Organic Chemistry
8th Edition
ISBN: 9781305580350
Author: William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher: Cengage Learning
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Chapter 27, Problem 27.51P
Interpretation Introduction
Interpretation:
In Merrifield solid phase peptide synthesis, the amino group is protected by fluorenylmethoxycarbonyl group (FMOC). The deprotection of the amino group is done by treatment with weak base such as secondary
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Using the information below, determine the amino acid sequence of the peptide, and explain how your structure is consistent with each piece of information.
Complete hydrolysis by 6 M HCl at 110°C followed by amino acid analysis indicated the presence of Gly, Leu, Phe, and Tyr in a 2:1:1:1 molar ratio.
Treatment of the peptide with1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found.
Complete digestion of he peptide with pepsin (which cleaves on the amino side of aromatic residues) followed by chromatography yielded a dipeptide containing Phe and Leu and a tripeptide containing Tyr and Gly in a 1:2 ratio.
Somatostatin is a tetradecapeptide of the hypothalamus that inhibits the release of pituitary growth hormone. Its amino acid sequence has been determined by a combination of Edman degradations and enzymic hydrolysis experiments. On the basis of the following data, deduce the primary structure of somatostatin: 1. Edman degradation gave PTH-Ala. 2. Selective hydrolysis gave peptides having the following indicated sequences: Phe-Trp Thr-Ser-Cys Lys-Thr-Phe Thr-Phe-Thr-Ser-Cys Asn-Phe-Phe-Trp-Lys Ala-Gly-Cys-Lys-Asn-Phe 3. Somatostatin has a disulfide bridge.
A peptide has the following amino acid composition:
2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser
Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide produces fragments with the following sequences:
Fragment A: Glu-Gly-Lys-Phe
Fragment B: Met-Ser-Leu-Arg
Fragment C: Met-Val-Glu-Phe
What information do this result give about the sequence of the peptide? Explain how you arrived on your answer.
a) The sequence is: Met-Val-Glu-Phe-Glu-Gly-Lys-Phe-Met-Ser-Leu-Arg
b) The sequence is: Met-Ser-Leu-Arg-Met-Val-Glu-Phe-Glu-Gly-Lys-Phe
c) The sequence is: Met-Val-Glu-Phe-Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe
d) The sequence is: Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe-Met Val-Glu-Phe
Chapter 27 Solutions
Organic Chemistry
Ch. 27.1 - Of the 20 protein-derived amino acids shown in...Ch. 27.2 - Prob. 27.2PCh. 27.2 - Prob. 27.3PCh. 27.3 - Draw a structural formula for Lys-Phe-Ala. Label...Ch. 27.4 - Which of these tripeptides are hydrolyzed by...Ch. 27.4 - Deduce the amino acid sequence of an undecapeptide...Ch. 27.6 - Prob. 27.7PCh. 27 - What amino acid does each abbreviation stand for?...Ch. 27 - The configuration of the chiral center in -amino...Ch. 27 - Assign an R or S configuration to the chiral...
Ch. 27 - Prob. 27.11PCh. 27 - Prob. 27.12PCh. 27 - Draw zwitterion forms of these amino acids. (a)...Ch. 27 - Prob. 27.14PCh. 27 - Why is Arg often referred to as a basic amino...Ch. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Both norepinephrine and epinephrine are...Ch. 27 - Prob. 27.22PCh. 27 - Draw a structural formula for the form of each...Ch. 27 - Prob. 27.24PCh. 27 - Write the zwitterion form of alanine and show its...Ch. 27 - Prob. 27.26PCh. 27 - Write the form of aspartic acid most prevalent at...Ch. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - For lysine and arginine, the isoelectric point,...Ch. 27 - Prob. 27.31PCh. 27 - Account for the fact that the isoelectric point of...Ch. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - At pH 7.4, the pH of blood plasma, do the majority...Ch. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - A chemically modified guanidino group is present...Ch. 27 - Draw a structural formula for the product formed...Ch. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - A decapeptide has the following amino acid...Ch. 27 - Following is the primary structure of glucagon, a...Ch. 27 - Prob. 27.45PCh. 27 - Draw a structural formula of these tripeptides....Ch. 27 - Estimate the pI of each tripeptide in Problem...Ch. 27 - Glutathione (G-SH), one of the most common...Ch. 27 - Following are a structural formula and a...Ch. 27 - Prob. 27.50PCh. 27 - Prob. 27.51PCh. 27 - Prob. 27.52PCh. 27 - Prob. 27.53PCh. 27 - Prob. 27.54PCh. 27 - Distinguish between intermolecular and...Ch. 27 - Prob. 27.56PCh. 27 - Prob. 27.57P
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- Determine the amino acid sequence of a polypeptide from the following data: Complete hydrolysis of the peptide yields Ala, Arg, Gly, 2 Lys, Met, Phe, Pro, 2 Ser, Tyr, and Val. Treatment with Edman’s reagent releases PTH-Val. Carboxypeptidase A releases Ala. Treatment with cyanogen bromide yields the following two peptides: 1. Ala, 2 Lys, Phe, Pro, Ser, Tyr 2. Arg, Gly, Met, Ser, Val Treatment with trypsin yields the following three peptides: 1. Gly, Lys, Met, Tyr 2. Ala, Lys, Phe, Pro, Ser 3. Arg, Ser, Val Treatment with chymotrypsin yields the following three peptides: 1. 2 Lys, Phe, Pro 2. Arg, Gly, Met, Ser, Tyr, Val 3. Ala, Serarrow_forwardAn unknown decapeptide was isolated and characterized. Complete hydrolysis of this peptide gave : F(2), A,G,C,K,N,T, W and V. Treatment with carboxypeptidase releases A. Reaction with Edman’s reagent gave PTH-T and a nonapeptide. The nonapeptide was treated with trypsin and gave 2 peptides: (V-C-G-A) and (N-FF-W-K). Give the sequence of amino acid in the decapeptide.arrow_forwardWrite out the steps needed to synthesize the following peptide using the Merrifield method.arrow_forward
- The peptide Proline-Serine-Alanine-Phenylalanine-Glutamine is present at pH 7. Draw the peptide and include stereochemistry.arrow_forwardAn amino acid residue side chain is deprontonated at pH9.5. What is the pKa of this residue if it is fully deprotonated at this pH?arrow_forwardShow the mechanism and explain how the Ala-Val-Ile peptide bond is formed.arrow_forward
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