Biological Science (6th Edition)
6th Edition
ISBN: 9780321976499
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Emily Taylor, Greg Podgorski, Jeff Carmichael
Publisher: PEARSON
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Chapter 3, Problem 13PIAT
Summary Introduction
To determine:
The frequency of proline to appear in peptide, if it were made up of a completely random assortment of the 20 most common amino acids
Given:
One of the peptides that can be recovered after gluten digestion is 33 residues long; 13 of the 33 residues are proline.
Introduction:
Gluten proteins are rich in amino acid proline, so they do not break down easily during digestion in small intestine, resulting in short and long peptides. These peptides can be broken down further and absorbed through the intestine and further can be utilized by the body.
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Chapter 3 Solutions
Biological Science (6th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site?
a. the location in an...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYUCh. 3 - Prob. 9TYPSSCh. 3 - 10. Make a concept map (see BioSkills 12) that...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Why different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?arrow_forwardSolve only the specific amino acid number and percent (%) Difference. Thank you so much♥arrow_forwardIn a sample solution given to be analyzed; Starch + Val-Gly-Ile-Trp-Lys-Gly-Ala-Gly-Val-Glu Plan a chain of tests to prove the presence and quantity of the peptide sequence. In the meantime, pay attention to the variety of methods that can be used and explain their basic principles.arrow_forward
- Identify and briefly describe the different PEGylation strategies you can use to PEGylate this peptide and draw the chemical structure of the resulting mPEG peptide conjugates.arrow_forwardWhat kind of information is stored in protein three-dimensional structure. Why 3D structure prediction is important? In detail discuss the major factors involved in 3D protein structure prediction and evaluation computationally.arrow_forwardAutomated amino acid analysis of peptides containing asparagine (Asn) and glutamine (Gln) residues gives a peak corresponding to ammonia. Why?arrow_forward
- Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12arrow_forwardSuppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture. What will be the expected result if a biochemist does an end-group analysis to identify the N and C terminal residues of the protein? Explain why.arrow_forwardPeptide A: AFEQHSR Calculate the isoelectric point of Peptide A using the pKa values in Table 4-1 of Voet, Voet and Pratt. Assume that the pKa values for the N-terminal amino group and C- terminal carboxyl groups are 8.0 and 3.5, as previously discussed in class. 3.785 5.055 7.02 10.24 3.50arrow_forward
- Give typing answer with explanation and conclusion On paper draw a dipeptide, clearly showing the peptide bond joining the two amino acids together. If the two amino acids are valine and threonine, predict the overall charge of the dipeptide at pH 7. Do not forget to consider the amino (N-terminal) and carboxy (C-terminal) of the dipeptide, as well as the R groups. Select one: a. +2 b. -2 c. 0 d. -1 e. +1arrow_forward01 Description Please draw the structure of the 19 L-a-amino acids and proline in any form, as you prefer. You may want to use a letter-size sheet or larger, it's up to you. Guiding principle: You want to understand the differences among amino acids. Although you may want to only draw the R-group it's preferable to draw it along with the rest of the molecule (i.e., the Ca, the amino group and the carboxyl group). Here are some examples (your drawings should not limited to the following styles): NH₂ OH Alanine H H O OH Proline lysine alarmy stock płwłos Tryptophan OH COOH | H₂N-C-H CH₂ Phenylalanine argininearrow_forwardCan Hydrophobic Interaction Bead Chromatography be used to isolate Protein X from muscle tissue if Protein X contains many hydrophobic regions? Explain the process of how to isolate Protein X from muscle tissue.arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY