/*! This file is auto-generated */ .wp-block-button__link{color:#fff;background-color:#32373c;border-radius:9999px;box-shadow:none;text-decoration:none;padding:calc(.667em + 2px) calc(1.333em + 2px);font-size:1.125em}.wp-block-file__button{background:#32373c;color:#fff;text-decoration:none} 21-50P Show the peptides that would res... [FREE SOLUTION] | 91影视

91影视

Log out

Learning Materials

Features

Discover

Chapter 21: 21-50P (page 1026)

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

Short Answer

Expert verified
  1. Val-Arg-Gly-Met-Arg-AlaSer
  2. Ser-Phe-Lys-Met Pro-Ser-Ala-Asp
  3. ArgSer-Pro-Lys Lys Ser-Glu-Gly

Step by step solution

01

Specificity of carboxypeptidase A in protein cleavage

Carboxypeptidase A is specific to breaking the C-terminal amino acid. Therefore, the bond-breaking sites are:

Val-Arg-Gly-Met-Arg-Ala*-Ser

02

Specificity of cyanogen bromide in protein cleavage

Cyanogen bromide hydrolysis is on the C side of a Met. Therefore, the site of bond breaking is represented by *:

Ser-Phe-Lys-Met*-Pro-Ser-Ala-Asp

03

Specificity of trypsin in protein cleavage

Trypsin hydrolysis is the C-side of Arg and Lys. Therefore, the breaking of the bond takes place after Arg and Lys make three chain.

Arg*-Ser-Pro-Lys*-Lys-Ser-Glu-Gly

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 91影视!

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

a.Which amino acid has the lowest pI value?

b.Which amino acid has the highest pI value?

c.Which amino acid has the greatest amount of negative charge at pH = 6.20?

d.Which amino acid has a greater negative charge at pH = 6.20, glycine or methionine?

Draw the resonance contributors of the peptide bond in the less stable configuration.

Alanine has pKa values of 2.34 and 9.69. Therefore, alanine exists predominately as a zwitterion in an aqueous solution with pH > ____ and pH < ____.

Explain why cyanogens bromide does not cleave on the C-side of cysteine.

Explain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a column packed with Dowex 50 (Figure 21.3):

a. aspartate before serine c. valine before leucine

b. serine before alanine d. tyrosine before phenylalanine
See all solutions

Recommended explanations on Chemistry Textbooks

Chemical Analysis

Read Explanation

The Earths Atmosphere

Read Explanation

Ionic and Molecular Compounds

Read Explanation

Physical Chemistry

Read Explanation

Nuclear Chemistry

Read Explanation

Kinetics

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.