Draw the entire structure of the amino acid product (with the correct stereochemistry) that results from the following chemical transformations. If no reaction occurs then just draw the structure of the starting material.

Draw the entire structure of the amino acid product (with the correct stereochemistry) that results from the following chemical transformations. If no reaction occurs then just draw the structure of the starting material.

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.SE: Something Extra

Problem 45AP

See similar textbooks

Related questions

Q: Draw structures to show the product formed in each case when lysine reacts with an excess of aqueous…

A: Interpretation- To draw the structure when lysine reacts with an excess of aqueous HCl.…

Q: A tripeptide undergoes complete hydrolysis and the resulting mixture contains only phenylalanine and…

Q: Ninhydrin reacts with an amino acid to form a purple-colored compound. Propose a mechanism to…

Q: a) Explain why the acetamido group is an ortho, para-directing group. Why should it be less…

A: As there are two questions, we have solved the first question for you, and for the rest to be solved…

Q: Why can isomaltose be easily hydrolyzed through acid hydrolysis while trehalose cannot undergo acid…

A: Carbohydrate chemistry:

Q: Explain the process of protein de maturation with an appropriate example

A: Biomolecules can be defined as the molecules which are involved in different biochemical reactions…

Q: α-Amino acids can be prepared by treating an aldehyde with ammonia/trace acid, followed by hydrogen…

A: α-Amino acids is prepared by treating 3-methylbutanal with ammonia/trace acid, followed by hydrogen…

Q: Histamine is synthesized from one of the 20 protein-derived amino acids. Suggest which amino acid is…

Q: Define tautomerism and use one of the structures above to illustrate your explanation

Q: 1. Name the common amino acids that contain an aromatic ring. Enter your answers in alphabetical…

A: Since you have asked multiple question, we will solve the first question for you. If you want any…

Q: Why is only a trace amount of acid used in the formation of an N-glycoside?

A: N-glycoside is prepared from sugar (monosaccharide) when reacts with amine in presence of traces of…

Q: Show the formation of the sphingolipid containing oleic acid, phosphoric acid, and choline.

A: Sphingolipids are a class of biomolecular compounds that are composed of fatty acid derivatives of…

Q: Explain why the rate of aminolysis of an ester cannot be increased by H+, HO-, or RO-.

A: The presence of acid, base and alkoxide ion does not increase the rate of Aminolysis reaction. The…

Q: Prepare valine from the corresponding: a) aldehyde, b) halocarboxylic acid, c) keto acid, d) nitro…

A: “Since you have posted a question with multiple sub-parts, we will solve first three subparts for…

Q: If anisole is allowed to sit in D2O that contains a small amount of D2SO4, what products are formed?

A: Structure of anisole is as follows, The compound anisole is an organic compound that is colorless…

Q: Compound A is a D-aldopentose that can be oxidized to an optically inactive aldaric acid B. On…

A: The class of D-aldopentoses includes five-carbon, aldehyde functional group-containing…

Q: Draw the structure of alanine in a solution at pH = 0

A: To find: The structure of alanine in a solution at pH=0

Q: Draw the condensed structures of the given amino acids. Glycylserine and Serylglycine Draw the…

Q: Consider the following tetrapeptide, written in a sequence according to normal convention, from left…

A: # Option-1: Disulfide linkage is formed by sulfur containing amino acid cysteine. Since Residue 2…

Q: At its pK, what percentage of boric acid is ionized? 50%. 75%. 25%. 100%. 10%. QUESTION 2 The side…

A: For the first Question, you can used the Hinderson equation for determination the percentage of…

Q: How many aldaric acids are obtained from the 16 aldohexoses?

A: Aldaric acid is the acid having both end of the molecule equivalent due to which the position of…

Q: -NH 'N- H,N. NH HN HN `Ph HO, HN. HN" H2N -Ph: Phenyl group, -C6H5 `NH

Q: Would you expect fructose or glucose to form a red color rapidly with Seliwanoff’s reagent? Explain…

A: Concept is based on practical carbohydrate chemistry.

Q: How do you synthesize the amino acid Phenylalanine from benzaldehyde as the starting compound?…

A: Following is the preparation of Phenylalanine from benzaldehyde.

Q: Show the formation of the sphingolipid containing stearic acid, phosphoric acid and choline

A: Sphingolipid belongs to the categories of phospholipids which consists fatty acids (R-COOH),…

Q: The aminolysis of acetic anhydride will produce aniline and ammonia as major products. True or…

Q: One of the ways in which an L a-amino acid can be synthesized is to carry out an Sy2 reaction…

A: Stereoisomer is the isomers of the compound with two non-superimposable images of the given…

Q: The amino group is an activator in electrophilic aromatic substitution. O True O False

Q: Perform a retrosynthetic analysis on the following peptide from the given starting materials.

A: The given peptide is,

Q: Draw the products from Killiani-Fischer reaction of D-ribose and L-Xylose.

A: Kiliani fischer synthesis is a chain elongation reaction of carbohydrates in which we synthesize a…

Q: Show how you would use the Strecker synthesis to make tryptophan

A: Strecker synthesis : It is a condensation reaction of an aldehyde with ammonium chloride (NH4Cl )…

Q: Write out a stepwise sequence that shows how a racemic mixture of leucine enantiomers can be…

A: The given recemic mixture of leucine enantiomers. The (S)-form and (R)-forms react with the given…

Q: Another method to form a peptide bond involves a two-step process:[1] Conversion of a Boc-protected…

A: a) Nitro group is an electron withdrawing group. Here nitro group is present on para position of the…

Q: Illustrate the Generation of the electrophile (CH3CO)+

A: An electron deficient species is termed as an electrophile. Electrophile are generally positively…

Q: Which of the following is true for structure II? L-ketose D-ketose D-aldose L-aldose

A: The name of the structure depends on the the functional group present in the structure . The prefix…

Q: structure of beta anomers of alpha D- mannopyranose and give their names

Q: alpha-Amino acids can be prepared by treating an aldehyde with ammonia/trace acid, followed by…

A: Strecker synthesis is a method of synthesize α-amino acids by treating an aldehyde with…

Q: amino NH H20 HN + NHg tautomerism H. wracil cytorine

A: The reaction given is,

Q: Draw the form of L-lysine which is present at biological pH.

A: form of L-lysine which is present at biological pH =7.4

Q: Suggest a test you will use to show that a given food substance contains protein. Show how you will…

A: The Biuret solution is a blue colour reagent which when comes in contact with the proteins, converts…

Q: Choose one structure below that best represents a lipid that can be used as starting material for…

Q: C17H29COOH linolenic acid non-saponifiable w-3 fatty acid All are correct

Q: sters can be cleaved in acidic conditions (hydrolysis) or in basic conditions (saponification), but…

A: In esterification, an acid and an alcohol undergo condensation reaction to form an ester.

Concept explainers

Designing a Synthesis

Organic synthesis is a branch of chemical synthesis that involves the planned construction of organic compounds/molecules from smaller units that possess functional groups. Friedrich Wöhler was the first scientist who designed the synthesis of an organic compound, urea from inorganic starting materials silver cyanate with ammonium chloride via a simple, one-step synthesis.

Question

Draw the entire structure of the amino acid product (with the correct stereochemistry) that results
from the following chemical transformations. If no reaction occurs then just draw the structure of the
starting material.
H2, Pd/C, ETOH
Cbz-L-Trp(Boc)OBn
50% TFA, CH2CI2
Вос-D-Lys(Cbz)OAlyl
На, cat. Pd/C
Fmoc-L-Tyr(tBu)OMe
20% piperidine-CH2CI2
Fmoc-L-Asp(OtBu)OBn
cat. Pd(PPH3)4
Alloc-D-His(Trt)OAllyl
morpholine

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1

Step 2

Step 3

Step 4

Step 5

Step by step

Solved in 5 steps with 5 images

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.

Similar questions

Draw the structure of the tetrapeptide Asp-Arg-Val-Tyr. Please show the appropriate stereochemistry of the natural amino acids in the resulting peptide. Please draw all ionizable groups in their neutral form.
An 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.
A tripeptide on hydrolysis produced glycine, alanine and leucine. The structures of these amino acids are shown below. On reaction with Edman’s reagent, leucine was released as the phenylhydantoin. Treatment of the tripeptide with carboxypeptidase gave glycine. Draw the structure of the tripeptide.
Glutamic acid is a naturally occurring α-amino acid that contains acarboxy group in its R group side chain. (Glutamic acid isdrawn in its neutral form with no charged atoms, a form that does not actually exist at any pH.) a.) What form of glutamic acid exists at pH = 1?b.) If the pH is gradually increased, what form of glutamic acid exists afterone equivalent of base is added? After two equivalents? After threeequivalents?c.) Propose a structure of monosodium glutamate, the common flavorenhancer known as MSG.
Give the amino acid sequence of hexapeptides that produce the following sets of fragments upon partial acid hydrolysis: (a) Arg, Gly, Ile, Leu, Pro, Val gives Pro-Leu-Gly, Arg-Pro, Gly-Ile-Val (a) N, L, M, W, V2 gives V-L, V-M-W, W-N-V
A nonapeptide released by globulins in the blood in response to a waspsting. Hydrolysis gives the following amino acids: 2 Arg, Gly, 2 Phe, 3 Pro, and Ser.Edman degradation gives phenylthiohydantoin of Arg. Cleavage with carboxypeptidase gives Arg. Partial hydrolysis gives the following di- and tripeptides: Phe-Ser, Pro-GlyPhe, Pro-Pro, Ser-Pro-Phe, Phe-Arg, and Arg-Pro. What is the amino acid sequence of this peptide?
Write out the steps needed to synthesize the following peptide using the Merrifield method.
Protein: SHAYNERSE Predict the products of the following reactions with the protein given, if there is none, write NO RXN. - Biuret reagent - KOH/Pb(CH2COO)2 - Glyoxilic Acid/Conc. H2SO - Hg/HNO3 - HNO3
This is a homework question... In nature, amino acids in proteins are typically found in the L-configuration. This is basedon it’s relationship to D- and L-glyceraldehyde. Shown below is the structure of the amino acidasparagine (Asn) at physiological pH. As written does histidine have an L(S)- or D(R)-configuration? Be sure to show how you derived your answer:
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 + RP
What is the correct structure for the peptide SGHKRY at pH 5.0?
Determine the amino acid sequence of a polypeptide from the following data:Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val.Carboxypeptidase A releases Val.Edman’s reagent releases PTH-Leu.Treatment with cyanogen bromide gives three peptides with the following amino acid compositions:1. His, Lys, Met, Pro, Ser 2. Thr, Val 3. Ala, Arg, Leu, Lys, Met, Ser