Log out Go to App
Go to App

Learning Materials

Features

Discover

Chapter 24: Q12P (page 1270)

Show how you would use a Strecker synthesis to make

  1. Leucine (b) Valine (c) Aspartic acid

Answer

Short Answer

Expert verified

(a)

Formation of leucine

(b)

Formation of valine

(c)

Formation of aspartic acid

Step by step solution

01

Formation of amino acids by Strecker synthesis

In Strecker synthesis, an aldehyde is treated with ammonia NH3,and then the addition of hydrogen cyanide HCN takes place,followed by hydrolysis H3O+to form the respective amide.

02

(a)

The Strecker synthesis for leucine is shown by the reaction given below:

Formation of leucine

(b)

The Strecker synthesis for valine is shown by the reaction given below:

Formation of valine

(c)

The Strecker synthesis for aspartic acid is shown by the reaction given below:

Formation of aspartic acid

Unlock Step-by-Step Solutions & Ace Your Exams!

  • Full Textbook Solutions

    Get detailed explanations and key concepts

  • Unlimited Al creation

    Al flashcards, explanations, exams and more...

  • Ads-free access

    To over 500 millions flashcards

  • Money-back guarantee

    We refund you if you fail your exam.

Start your free trial

Over 30 million students worldwide already upgrade their learning with Vaia!

One App. One Place for Learning.

All the tools & learning materials you need for study success - in one app.

Get started for free

Most popular questions from this chapter

Show the steps and intermediates in the synthesis of Leu-Ala-Phe by the solid-phase process.

Show where trypsin and chymotrypsin would cleave the following peptide.

Tyr-Ile-Gln-Arg-Leu-Gly-Phe-Lys-Asn-Trp-Phe-Gly-Ala-Lys-Gly-Gln-Gln.NH2

Show how solid-phase peptide synthesis would be used to make Ile-Gly-Asn.

Peptides often have functional groups other than free amino groups at the N terminus and other than carboxyl groups at the C terminus.

(a) A tetrapeptide is hydrolyzed by heating with 6 M, and the hydrolysate is found to contain Ala, Phe, Val, and Glu. When the hydrolysate is neutralized, the odor of ammonia is detected. Explain where this ammonia might have been incorporated in the original peptide.

(b) The tripeptide thyrotropic hormone releasing factor(TRF) has the full name pyroglutamylhistidylprolinamide. The structure appears here. Explain the functional groups at the N terminus and at the C terminus.

(c)On acidic hydrolysis, an unknown pentapeptide gives glycine, alanine, valine, leucine and isoleucine. No odor of ammonia is detected when the hydrolysate is neutralized. Reaction with phenyl isothiocyanate followed by mild hydrolysis gives nophenylthiohydantoin derivative. Incubation with carboxypeptidase has no effect. Explain these findings.

There are many methods for activating a carboxylic acid in preparation for coupling with an amine. The following method converts the acid to an N-hydroxysuccinimide (NHS) ester.

(a) Explain why an NHS ester is much more reactive than a simple alkyl ester.

(b) Propose a mechanism for the reaction shown.

(c) Propose a mechanism for the reaction of the NHS ester with an amine, R-NH2
See all solutions

Recommended explanations on Chemistry Textbooks

Organic Chemistry

Read Explanation

Chemical Analysis

Read Explanation

Ionic and Molecular Compounds

Read Explanation

Inorganic Chemistry

Read Explanation

Making Measurements

Read Explanation

Physical Chemistry

Read Explanation
View all explanations

What do you think about this solution?

We value your feedback to improve our textbook solutions.

Study anywhere. Anytime. Across all devices.

Sign-up for free