Organic Chemistry - Standalone book
10th Edition
ISBN: 9780073511214
Author: Francis A Carey Dr., Robert M. Giuliano
Publisher: McGraw-Hill Education
expand_more
expand_more
format_list_bulleted
Question
Chapter 26, Problem 43P
Interpretation Introduction
Interpretation:
The mechanisms for the rearrangement and coupling steps are to be written in NCL for the given reaction.
Concept Introduction:
The sulfur atom in the side chain of cysteine acts as a nucleophile and can attack the carbonyl carbon of the thioester of an amino acid.
The non-native thioester linkage in the product undergoes a rearrangement in order to form a more stable amide linkage.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Which of the following reagents can be used to cleave a tert-butoxycarbonyl (Boc) protecting group from a peptide?
H₂/Pd
CF3CO₂H
Na₂CO3, H₂O
LiAlH4
B
Reaction of the a-carboxyl group of an amino acid or peptide with phenylisothiocyanate allows for the determination of the amino acid residue in the N-
terminus of an unknown peptide
O True
O False
Treatment of a new protein with dansyl chloride reveals two (2) dansyl-labelled derivatives of amino acids, alanine and methionine. What can you deduce about the structure of the proteinfrom these results?
Chapter 26 Solutions
Organic Chemistry - Standalone book
Ch. 26.1 - Prob. 1PCh. 26.2 - Prob. 2PCh. 26.2 - Prob. 3PCh. 26.3 - Prob. 4PCh. 26.3 - Prob. 5PCh. 26.4 - Prob. 6PCh. 26.4 - Prob. 7PCh. 26.4 - Prob. 8PCh. 26.5 - Prob. 9PCh. 26.6 - Prob. 10P
Ch. 26.6 - Prob. 11PCh. 26.6 - Prob. 12PCh. 26.7 - Prob. 13PCh. 26.7 - Prob. 14PCh. 26.7 - Prob. 15PCh. 26.7 - Prob. 16PCh. 26.7 - Prob. 17PCh. 26.9 - Prob. 18PCh. 26.10 - Digestion of the tetrapeptide of Problem 26.18...Ch. 26.12 - Prob. 20PCh. 26.12 - Prob. 21PCh. 26.15 - Prob. 22PCh. 26.15 - Prob. 23PCh. 26.16 - Prob. 24PCh. 26.17 - Prob. 25PCh. 26.18 - Prob. 26PCh. 26 - Prob. 27PCh. 26 - Prob. 28PCh. 26 - Prob. 29PCh. 26 - Prob. 30PCh. 26 - Prob. 31PCh. 26 - Prob. 32PCh. 26 - Prob. 33PCh. 26 - Prob. 34PCh. 26 - Prob. 35PCh. 26 - Prob. 36PCh. 26 - Prob. 37PCh. 26 - Prob. 38PCh. 26 - Prob. 39PCh. 26 - Prob. 40PCh. 26 - If you synthesized the tripeptide Leu-Phe-Ser from...Ch. 26 - Prob. 42PCh. 26 - Prob. 43PCh. 26 - Prob. 44PCh. 26 - Prob. 45DSPCh. 26 - Prob. 46DSPCh. 26 - Prob. 47DSPCh. 26 - Prob. 48DSPCh. 26 - Prob. 49DSPCh. 26 - Prob. 50DSP
Knowledge Booster
Similar questions
- Bradykinin is a linear nonapeptide released by blood plasma globulin in response to a wasp sting. It is a very potent pain-causing agent. Its constituent amino acids are 2R, G, 2F, 3P, S. The sue of 2,4-dinitrofluorobenzene and carboxypeptidase shows that both terminal residues are arginine. Partial hydrolysis of bradykinin gives the following di- and tripeptides: FS + PGF +PP + SPF + FR + RParrow_forwardEthyleneimine reacts with cysteine side chains in proteins to form S - aminoethyl derivatives. The peptide bonds on the carboxyl side of these modified cysteine residues are susceptible to hydrolysis by trypsin . Why?arrow_forwardThe first step in the catabolism of most amino acids is the removal of the nitrogen atom by transfer to an a-keto acid, a reaction catalyzed by an enzyme called a transaminase. The a-keto acid acceptor is often a-ketoglutarate. Modify the structures in the product to show the products of the transamination of cysteine. Be sure to show functional groups with the charge and number of attached hydrogen atoms appropriate for pH 7.4. transaminase + O=C H₂N-CH + CH₂ CH₂ CH₂ SH Incorrect H₂N || CH | CH₂ | CH₂ I || O || n | CH₂ T SHarrow_forward
- There are 20 common, naturally occurring amino acids from which all proteins are derived (as will be discussed in Chapter 25), although many other less common amino acids have been isolated from natural sources. Valine is one of the 20 common amino acids, and it was used as a starting material in the laboratory synthesis of an uncommon amino acid (Tetrahedron 1997, 53, 1151-1156). During one of the steps in the synthesis, compound 1 was treated with HBr under conditions that favor radical addition, giving stereoisomers 2 and 3. Draw the structures of 2 and 3, and describe their stereoisomeric relationship. H. LOCH3 HBr 2 + 3 hv H (S)-valine Modify the given copies of compound 1 to drawthe structures of 2 and 3. You can use the single bond tool to add/remove double bonds. CH2 CH2 H,C- H3C- -CH, -CH, Edit Drawing Describe the relationship of 2 and 3. O They are enantiomers. O They are superimposable. They are diastereomers. O They are constitutional isomers.arrow_forwardConsider the following tetrapeptide, written in a sequence according to normal convention, from left to right: Residue 1 is acidic; Residue 2 is cysteine (an amino acid containing a –CH2SH R-group); Residue 3 is proline (a large hydrophobic amino acid); Residue 4 is basic. Of the following four general statements, which one is TRUE regarding this tetrapeptide? This tetrapeptide does not have the ability to form a disulfide linkage with an identical tetrapeptide. Residue 2 belongs to the amino acid category known as "basic." 3 of these 4 responses are correct This tetrapeptide could be part of an alpha-helix, since the large size of the proline would not have any impact on the consistency of the spiral shape. The acidic residue (Residue #1) is at the amino terminus of this tetrapeptide.arrow_forwardthe pKa values for phenylalanine are 1.83 (carboxyl group) and 9.13 (amino group). Use the Henderson-hasselbach equation to determine the ratio of the acidic and basic forms of each of the ionizing groups of phenylalanine at neutral pH. Based on this, draw the predominant structure of phenylalanine at neutral pH.arrow_forward
- N-(2-hydroxyethylpiperazine-N'-(2-ethanesulfonic A purified protein is in a Hepes acid) buffer at pH 7 with 475 mM NaCl. A dialysis membrane tube holds a 2.5 ml. sample of the protein solution. The sample tube floats in a beaker containing 1.75 L of the same Hepes buffer, but with 0 mM NaCl, for dialysis. Small molecules and ions (such as Na*, CI, and Hepes) can to diffuse across the dialysis membrane, but the protein cannot. Assume there are no sample volume changes during the dialysis. Calculate the final concentration of NaCl in the protein sample once the dialysis has come to equilibrium. [NaCl] after a single dialysis: mM Calculate the final NaCl concentration in the 2.5 ml. protein sample after dialysis in 175 mL of the same Hepes buffer. with 0 mM NaCl, twice in succession. [NaCl] after a double dialysis: mMarrow_forwardWhich of the attached amines can be used to resolve a racemic mixture of amino acids?arrow_forwardHistamine is synthesized from one of the 20 protein-derived amino acids. Suggest which amino acid is its biochemical precursor and the type of organic reaction(s) involved in its biosynthesis (e.g., oxidation, reduction, decarboxylation, nucleophilic substitution). CH,CH,NH, H. Histaminearrow_forward
- A normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutant poly peptide differ by one amino acid. The fingerprints of the peptides obtained from the two polypeptides are shown below. What kind of amino acid substitution occurred as a result of the mutation? (That is, is the substituted amino acid more or less polar than the original amino acid? Is its pI lower or higher?)arrow_forwardAnother method to form a peptide bond involves a two-step process Conversion of a Boc-protected amino acid to a p-nitrophenyl ester. Why does a p-nitrophenyl ester “activate” the carboxy group of thefirst amino acid to amide formation?arrow_forwardDetermine the primary structure of an octapeptide from the following data: Acid-catalyzed hydrolysis gives 2 Arg, Leu, Lys, Met, Phe, Ser, and Tyr. Carboxypeptidase A releases Ser. Edman’s reagent releases Leu. Treatment with cyanogen bromide forms two peptides with the following amino acid compositions: 1. Arg, Phe, Ser 2. Arg, Leu, Lys, Met, Tyr Trypsin-catalyzed hydrolysis forms the following two amino acids and two peptides: 1. Arg 2. Ser 3. Arg, Met, Phe 4. Leu, Lys, Tyrarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Organic ChemistryChemistryISBN:9781305580350Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. FootePublisher:Cengage Learning
Organic Chemistry
Chemistry
ISBN:9781305580350
Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher:Cengage Learning