Warning: foreach() argument must be of type array|object, bool given in /var/www/html/web/app/themes/studypress-core-theme/template-parts/header/mobile-offcanvas.php on line 20

A decapeptide undergoes partial hydrolysis to give peptides whose amino acid composition is shown. Reaction of the intact decapeptide with Edman’s reagent releases PTH-Gly. What is the sequence of the decapeptide?

1.Ala, Trp

2. Val,Pro,Asp

3. Pro, Val

4. Ala, Glu

5. Trp, Ala, Arg

6.Arg, Gly

7.Glu, Ala, Leu

8. Met, Pro, Leu, Glu

Short Answer

Expert verified

The answer is,

Gly-Arg-Trp-Ala-Glu-Leu-Met-Pro-Val-Asp

Step by step solution

01

Step-by-Step Solution Step 1: Decapeptides

The decapeptides are peptides comprised of ten amino acids. The peptides are the amino acid chains interconnected by the peptide bond. The RCONHR’ bond is called the peptide bond. The peptides are composed of two, three, four, five, and ten amino acids known as a dipeptide, tripeptide, tetrapeptide, pentapeptide, and decapeptides.

02

Explanation

The N-terminal aminoacid is Gly. Look for a peptide fragment that contains Gly.

Fragment 6 tells that the second amino acid is Arg.

Fragment 5 tells that the next two can be Trp-Ala or Ala-Trp.

Fragment 4 tells that the Glu is next to the Ala. So the third and fourth ones will be Trp-Ala, and the fifth one is Glu.

Fragement 7 tells that the sixth amino acid is Leu.

Fragement 8 tells that the next two are Met-Pro or Pro-Met.

Fragment 3 tells that Pro is next to Val, so the seventh and eighth amino acids must be Met-Pro, and the ninth one is Val.

Finally, fragment 2 tells that the last amino acid is Asp.

Therefore the amino acid sequence is shown below.

Gly-Arg-Trp-Ala-Glu-Leu-Met-Pro-Val-Asp

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.

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 peptides that would result from cleavage by the indicated reagent:

a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A

b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide

c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsin

Cells can also convert a-keto acids into amino acids, but because the reagents organic chemists use for this reaction are not available in cells, they carry out this reaction by a different mechanism

(a) What amino acid is obtained from the reductive amination of each of the following metabolic intermediates in a cell by reductive amination?

(b) What amino acids are obtained from the same metabolic intermediates when the amino acids are synthesized in the laboratory?

a. Calculate the overall yield of bradykinin when the yield for the addition of each amino acid to the chain is 70%.

b. What would be the overall yield of a peptide containing 15 amino acids if the yield for the incorporation of each is 80%?

A mixture of amino acids that do not separate sufficiently when a single technique is used can often be separated by two-dimensional chromatography.In this technique, the mixture of amino acids is applied to a piece of filter paper and separated by chromatographic techniques. The paper is then rotated90°,and the amino acids are further separated by electrophoresis, producing a type of chromatogram called a fingerprint.Identify the spots in the fingerprint obtainedfrom a mixture of Ser, Glu, Leu, His, Met, and Thr.

Why are the carboxylic acid groups of the amino acids more acidic

(pKa ~ 2) than a carboxylic acid such as acetic acid (pKa = 4.76)?

See all solutions

Recommended explanations on Chemistry Textbooks

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