Concept explainers
(a)
Interpretation: The sequence of amino acid for given peptide using the fragments obtained by partial hydrolysis of the peptide with acid is to be given.
Concept introduction: Peptide linkage is formed between the amino group of one amino acid and the carboxyl group of other amino acid with the loss of water molecule. Amino acids are naturally occurring compounds in which the amino group is present on the alpha carbon of carboxyl group. The name of amino acids is represented by the one-letter and three-letter abbreviations.
(b)
Interpretation: The sequence of amino acid for given peptide using the fragments obtained by partial hydrolysis of the peptide with acid is to be given.
Concept introduction: Peptide linkage is formed between the amino group of one amino acid and the carboxyl group of other amino acid with the loss of water molecule. Amino acids are naturally occurring compounds in which the amino group is present on the alpha carbon of carboxyl group. The name of amino acids is represented by the one-letter and three-letter abbreviations.
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Chapter 27 Solutions
CNCT ORG CHEM 6 2020
- Consider the tripeptide leucylvalyltryptophan. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has a basic side chain?arrow_forwardOn complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments: Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids?arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forward
- What special role does the amino acid cysteine have in the peptides vasopressin and oxytocin?arrow_forwardDrawing Peptide Structures Draw the tripeptide that would result from cysteine attaching to the previous dipeptide on the acidic side.arrow_forwardGlutathione (G-SH), one of the most common tripeptides in animals, plants, and bacteria, is a scavenger of oxidizing agents. In reacting with oxidizing agents, glutathione is converted to G-S-S-G. (a) Name the amino acids in this tripeptide. (b) What is unusual about the peptide bond formed by the N-terminal amino acid? (c) Write a balanced half-reaction for the reaction of two molecules of glutathione to form a disulfide bond. Is glutathione a biological oxidizing agent or a biological reducing agent? (d) Write a balanced equation for reaction of glutathione with molecular oxygen, O2 to form G-S-S-G and H2O. Is molecular oxygen oxidized or reduced in this process?arrow_forward
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