/*! 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} Q35P What is the structure of each am... [FREE SOLUTION] | 91影视

91影视

Log out

Learning Materials

Features

Discover

Chapter 29: Q35P (page 1192)

What is the structure of each amino acid at its isoelectric point: (a) alanine (b) methionine; (c)aspartic acid; (d) lysine?

Short Answer

Expert verified

Amino acids constitute primary importance as they carry out several functions. Numerous amino acids are present; however, the proteins are created from twenty amino acids.

Step by step solution

01

Step 1:Amino acid

Amino acids constitute primary importance as they carry out several functions. Numerous amino acids are present; however, the proteins are created from twenty amino acids.

02

Isoelectric point

The isoelectric point indicated as pI, impacts the solubility of a specific molecule at a particular pH. Proteins comprise a net positive charge at a pH less than pI. A net negative charge is present at a pH larger than pI.

03

Structure of each amino acid at the isoelectric point

The amino acid is found as a zwitterion at the isoelectric point. At the isoelectric point, the deprotonation of and the protonation of takes place.

(a)The structure of the amino acid, alanine at its isoelectric point can be given as:

(b)The structure of the amino acid, methionine at its isoelectric point can be given as:

(c)The structure of the amino acid, aspartic acid at its isoelectric point can be given as:

(d)The structure of the amino acid, lysine at its isoelectric point can be given as:

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

Use the given experimental data to deduce the sequence of an octapeptide that contains the following amino acids: Ala, Gly (2 equiv), His (2 equiv), Ile, Leu and Phe. Edman degradation cleaves Gly from the octapeptide, and carboxypeptidase forms Leu and a heptapeptide. Partial hydrolysis forms the following fragments: Ile-His-Leu, Gly, Gly-Ala-Phe-His, and Phe-His-Ile.

Tryptophan is not classified as a basic amino acid even though it has a heterocycle containing a nitrogen atom. Why is the N atom in the five-membered ring of tryptophan not readily protonated by acid?

Draw the structure of each peptide. Label the N-terminal and C-terminal amino acids and all amide bonds.

a. Val鈥揋lu

b. Gly鈥揌is鈥揕eu

c. M鈥揂鈥揟鈥揟

a. Draw the structure of the tripeptide A-A-A, and label the two ionizable functional groups.

b. What is the predominant form of A-A-A at pH=1?

c. The values for the two ionizable functional groups (3.39 and 8.03) differ considerably from the values of alanine (2.35 and 9.87;see table 29.1). Account for the observed differences.

Draw the structure of the N-phenylthiohydantoin formed by initial Edman degradation of each peptide: (a) Ala-Gly-Phe-Phe; (b) Val-Ile-Tyr.
See all solutions

Recommended explanations on Chemistry Textbooks

The Earths Atmosphere

Read Explanation

Kinetics

Read Explanation

Physical Chemistry

Read Explanation

Chemical Analysis

Read Explanation

Making Measurements

Read Explanation

Inorganic 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.